Chapter 20 16 Mysteries of Life

off course At this time, Pauling's attention frequently shuttled back and forth between politics and science.Political activities put him in a position of being attacked, and research became his means of escape from the pressure.Under the repeated urging of the publishing house, he completed the compilation of the simple version of "General Chemistry" in 1949.This book is more suitable for first-year college freshmen who are not up to the level of Caltech, so it has a wider audience. He dictated it on a tape recorder, asked his secretary to organize it, and then he did the final polishing.His other book titled "University Chemistry", which came out in 1950, was also a bestseller. In 1950, Pauling bought a new British-built two-seater green racing car as a birthday present for Eva Helen.

Pauling continued to think about the structure of proteins. In the spring of 1950, when the Vinbam case happened, Lawrence Bragg, John Kendrew, Max Perutz and others published a special paper in the "Proceedings of the Royal Academy of Sciences" entitled "The Polypeptide Chain Structure of Crystal Protein ".When Pauling saw this title, he was stunned: Could it be that the research team in Prague had made a breakthrough, picked up the laurels ahead of him, and clearly separated the atoms in a protein structure one by one? After reading the text, he felt better.This paper by the Prague group is very strange. There is no central topic in the whole text. It is like drying clothes on a laundry room rope. It lists the basic types of proteins in a patchwork, lacking convincing evidence. There is also no clear way to identify which type a specific protein belongs to.Some are helical structures, others are rotating chain structures.Pauling knew very well that almost any of these structures could not be easily denied chemically.Bragg and his research team did not clearly point out which structure it is, let alone make a clear conclusion on the final structure of the protein.They were only feebly acknowledging the archaic idea of ​​Astberg's folded ribbon structure.

In this article by the Prague group, Pauling also read between the lines some interesting content.The author of this article constructed various models of protein structures based on his own understanding of the relevant structural elements - Pauling noted with satisfaction that the author also specially adopted the detailed information on the shape and size of amino acids published by the California Institute of Technology. The forces that give it the final shape are also taken into account, and the concept of hydrogen bonds is also particularly emphasized.Pauling himself would have done the same.

Clearly, Bragg has learned something in the fifteen years since he was outcompeted by the Pauling Rule.The few days Pauling spent at the Cavendish Laboratory in 1948 also had a certain influence on him; shortly after Pauling's return, Prague's coarse to finer attention to Perutz and Kendrew The research method was supplemented, emphasizing the structure of the whole protein, and examining the structure of each amino acid one by one, as Pauling did. Pauling, however, can rest assured knowing that Bragg still doesn't know how to play the game of randomness correctly.In his 1950 paper, Bragg did not impose enough constraints in terms of chemical properties to sufficiently narrow the scope of thinking when making guesses about protein structures.For example, the British obviously did not believe that the peptide chain must remain rigid and straight. Almost all the models they imagined could be twisted or bent. Pauling thought this was impossible-this is why they imagined One reason for having twenty possibilities instead of just a few.On the other hand, they all attach a restriction that Pauling considers unnecessary.The Cavendish team thought that each complete turn in their model of the helix must contain an integer number of amino acids—probably three or four.Huggins also made this mistake in his 1943 paper, thinking it was an integer.The way of thinking is that since the protein helical structure undergoes a process of crystallization, its basic repeating unit—the so-called spatial combination—must exhibit a symmetry that can be described by integers.Since the alpha keratin helical structure is considered to be composed of a complete circle, then, repeating continuously along the chain, with the help of the thinking method of space combination symmetry, it is considered that the number of amino acids in each circle is an integer, that is As a matter of course; thus, each turn should start and end at the same phase point of the amino acid backbone.

But it wasn't obvious to Pauling.When he folded his paper spiral model at Oxford University, he focused on the chemical principles and did not pay attention to the crystallization scheme.The model he came up with sloppily did not involve the question of whether the number of amino acids in each circle is an integer.However, once he thought about it, he couldn't see why it had to be this way.After reading Bragg's 1950 paper, he began to remember that the conclusions about this integer were inextricably linked to the "magic number" penchant for protein researchers in the 1930s.It was the mistake of believing in this wonderful round number that led Lynch into a strange circle and couldn't extricate himself.Pauling believes that nature does not operate in that way, and does not necessarily create various life forms according to the requirements of mathematical equations; nature is much more lazy than this, and it is more opportunistic-nature likes to use the easiest way to travel , which requires the least amount of energy—and this is how the most stable chemical structures are built!

The Prague research group did not get the crown, but their thesis made Pauling return to the race track with full concentration.When he returned from England two years ago, proteins had been his highest priority, and he had ordered several researchers to step up their efforts: Corey and his colleagues were still at the forefront of the study of the structure of amino acids and small peptides. The world's leading position, their research results confirmed Pauling's idea that the peptide bond is straight; Corey and a research team also studied a complete globular protein, lysozyme, which they cut into tiny fragments, separated on the chromatogram, and studied one by one; Pauling instructed the researchers to incorporate atoms of common heavy elements such as mercury into protein chains for X-ray analysis; another new colleague, Jack Coker, Ward used a Tektronix electrophoresis apparatus to gather information on the charge distribution and general properties of globular proteins. In the winter at the turn of 1948 and 1949, Herman Branson, a visiting professor of physics, visited, and Pauling arranged for him to examine in detail the possible models of the protein helical structure, "see if I have missed anything .” This model must meet the two conditions proposed by Pauling: the peptide bond is straight, and the number of hydrogen bonds is the maximum.Importantly, Pauling removed a condition attached by the Prague research group.He told Branson that we have no reason to believe that the number of amino acids in each picture of the helical structure must be an integer.Branson, with the help of Winebaum (who at this time had not yet been charged with perjury), set to work using his mathematical knowledge and extremely precise modeling equipment, and on the subject of helical structures, constructed Dozens of different models.

At this point, Pauling turned his attention to other things.He became president of the American Chemical Society in January 1949, and political activities took up more of his working time.Research on sickle cell anemia has blossomed.In the months of late 1949 and early 195M, Pauling spent a lot of time and used the above results as a jumping off point in an attempt to tackle medical problems such as cancer and heart disease at the molecular level. “I feel confident that great strides will be made in the fight against disease by linking medical research more closely to the most advanced frontiers of basic science,” he writes, “and to do so, The only way to do that is to see medical research as an integral part of advancing basic science experimentation.” He hopes to create a place where young MDs like Itano can take an approach based on their understanding of molecular action. New methods of medical research.To this end, he began planning for a new building that would house a medical chemistry laboratory.The lab would be a frontier between his Klein chemistry lab and Biddle's Kerkhoff biology lab, and staff would come from both.He intends to conduct medical research with a new perspective.

In January 1950, with Biddle's help, Pauling formally proposed such a site to the Rockefeller Foundation.However, Weaver poured cold water on him, claiming that biology and chemistry should first strengthen their own research and not open up new battlefields.Besides, financing the construction of the building is not within the scope of the foundation's business.For weeks that spring, Pauling and Biddle spent weeks writing letters and traveling the streets of New York seeking funding from other foundations and pharmaceutical companies—they asked, for example, $1.5 million from the Kresge Foundation— However, their demands were all in vain.The two Caltech scholars found that philanthropists, like doctors, take the time to understand the concept of molecular disease. These people even think that "medical chemistry" is a "confusing" term. Terminology—not only has the disadvantages of ambiguity, but also has the suspicion of alarmism.They are only willing to give some small short-term grants to the Caltech research group.

With no hope of obtaining funding, Pauling could only go back and continue to study the helical structure of proteins.The fall before that, after a year of research by Branson and Wynbaum, they had come to the conclusion that proteins had only two helical structures—one of which Pauling had considered when he was at Oxford—and could not only Satisfy the two conditions of hydrogen bond maximization and peptide bond straightness, and make each atom close to each other without overlapping.In each turn of the helix, the tighter of the two structures has about 3.7 amino acids and the looser has 5.1 amino acids.Pauling already knew that proteins could have only two helical structures, but he still didn't want to make them public.It is still an old problem that he saw as early as in England: most scholars believe that the pitch is an important parameter of the helical structure, and the data obtained by X-ray reflection of alpha keratin is 5.1 angstroms.However, neither of these helical structures fit this data.The research work of Branson and Winebaum confirmed that the relatively tight helical structure that Pauling was thinking at this time is probably the structure of keratin, but the pitch is 5.4 Angstroms. "I was very firm in my belief that this structure should fit the X-ray data," recalls Pauling, "so I decided to wait."

But one of the helices envisioned by the Prague team, the one with four amino acids per turn, is already very close to the 3.7-amino-acid helix Pauling knew.Pauling felt that sooner or later they would revise their research methods. In the spring of 1950, Pauling once again devoted himself to protein research.He comprehensively inspected Corey's recent systematic analysis on the possible structure of proteins, and made models of related structures with real objects such as wires, balls, and rods.In a workshop at the California Institute of Technology, he carved a new and colorful model out of wood. The atoms were represented by spheres, each marked with a van der Waals radius, and there were many small holes in the side of the ball. In order to facilitate the connection between the various spheres.The entire model looks like a mass of soap bubbles—hence the name space-filling models.It was another Pauling innovation that became a standard teaching aid in thousands of chemistry laboratories and classrooms.In the process of making the model, Pauling strictly followed his own regulations for the protein structure, ensuring that all possible hydrogen bonds were not missed, every peptide bond was kept straight, and there was no artificiality between the various components. Tensile stress, and the atoms are not squeezed too tightly against each other.In this way, Pauling and Corey used the model to prove that the two helical structures of proteins are chemically feasible.This time, they also got some new revelations - one of the structures could be stretched in a certain way, which could show that the structure had the properties of a ribbon.But despite their refinement, a puzzling problem remained: the tighter of the two basic structures of the protein, which Pauling believed to be the structure of keratin, remained The data of 5.1 Angstroms obtained by X-ray reflection cannot be explained.According to Pauling's theoretical structure, it can be predicted that it is a reflection of 5.4 Angstroms.The difference between these two figures - equal to one-sixth of the width of a hydrogen atom - became the only obstacle for Pauling to win the honor of being the first person to reveal the structure of proteins.This obstacle may be more insurmountable than the Grand Canyon of Colorado.

In the summer and autumn of 1950, Pauling had been accused by Budenz and investigated by Caltech, but he continued to study this problem, trying to figure out the structure of some other proteins. In September 1950, Pauling learned that his former student (and Lynch disciple) David Harker, with the support of Irving Langmuir, was building an "East Coast Laboratory" dedicated to protein structure research, and received substantial funding.This matter greatly enhanced Pauling's sense of urgency, and the competition became more intense.He needs to work harder.To do this, he began using a method devised to harness the activity of dreams.From the time he went to bed with the lights out to the time he actually fell asleep, he kept running through the questions that puzzled him the most.He found that using this method, his subconscious mind could continue working on the problem through the night.In his dreams, the protein helix was constantly tumbling and spinning, appearing and disappearing, erratic.This approach also made it possible for him not to have those nightmares of political persecution. However, all this does not bring any hope of solving the 5.1 Angstrom puzzle.So Pauling made a decision of great importance.Feeling "involuntarily bound by the papers of Bragg, Kendrew, and Perutz", Pauling decided to ignore the important information that contradicted the experimental results and at least publish a preliminary note-taking article on Talk about the model you envision for proteins.If he is right—that is, if he can find some undiscovered explanation for the discrepancy between his model and the X-ray data—he should first publish his results. If he is wrong, it does not matter when it was published. On October 16, 1950, Pauling and Corey sent a brief note to the Journal of the American Chemical Society stating that they were the first to obtain the relevant results.As mentioned in the article, they imagined two helical models: in one helical structure, the number of amino acid residues contained in each turn is 3.7; in the other structure, this number is 5.1.They also mention the arrangement of the hydrogen bonds, claiming to have found very strong evidence that the two structures they propose exist in a wide variety of proteins.The text also hints that they have made concrete models of silk.These are the gist of this note.At the end, the authors promise to "soon publish the results of their research in detail." The good news finally arrived unexpectedly.Pauling obtained new information from a man-made fiber manufacturing company called "Kotolz" in the United Kingdom.The company's researchers succeeded in generating completely artificial polypeptide chains made of only one type of amino acid.Compared with natural keratin, the characteristics of this artificial polypeptide chain are exactly the same in some respects, but significantly different in others.The Kotorz ​​researchers found that the artificial chain they had generated resembled many pencils bundled together in a box—evidence of a helical structure, according to Pauling, with an overall shape like An elongated cylinder -- they also found that there appeared to be hydrogen chains along the length of this chain.The best news, of course, came from the extremely fine X-ray images provided by the researchers: The new fibers showed no reflection at 5.1 angstroms. Pauling was very excited.It seems that this is a spiral structure - more precisely, a "spiral", at this time, Pauling has begun to use this name.The term was first coined and suggested to Pauling by one of his postdoc classmate Jack Doñez—although there is still no evidence for just how big that nerve-wracking distance is.Maybe the 5.1 Angstrom reflection in natural keratin is not as important as everyone thinks, maybe it is just an artificial phenomenon, or it is the result of a higher-level structure in natural keratin.In short, he was quite justified in ignoring it.Pauling and Corey regained their spirits and continued with the modeling, constructing the final forms of the two spirals.Pauling called the tight one the alpha helix, and the loose one the nima helix.Pauling and Corey also named the two filamentous extensions as sheets. News spread at Caltech: Pauling's group was building elaborate models of proteins.This caught the attention of the biologists at the Polytechnic Institute.That winter,.Pauling presented his ideas to them in a seminar.The large lecture hall of Kerkhoff Laboratory was full of seats, and the audience present were discussing a lot. "Everyone knew it was going to be a really high-profile hot issue," recalls biology professor Ray Owen. As usual, Pauling gave a lively speech.The assistants carried various brackets on their shoulders and surrounded him into the report hall.A tall object, covered with cloth and tied with a rope, seemed to be a statue about to be unveiled.Everyone knows that is the "model".Pauling began to give a speech. First, he introduced the basic situation of protein structure one by one, and at the same time drew some graphics to illustrate the important role of hydrogen chains and planar peptide chains.Holding a pile of soft plastic children's play beads, he snapped them together to see how the individual amino acids were connected.After making the necessary introductions, he got up and walked over to the model, took a jackknife from his pocket and opened it, as if to cut the string that was tied to it.Many people in the audience got up from their seats, staring at the scene that was about to happen.At this time, Pauling, the master performer, seemed to have remembered something, and set off to return to his original place.Everyone sat back in their seats.Noticing something of this effect, Pauling repeated the trick several times. "He really built a lot of suspense," Irving said. Afterwards, Pauling felt satisfied, and with a wave of his hands, the veil was lifted: a colorful, beautiful and moving model was revealed in front of people.This is the kind of tight helix he envisioned for proteins, known as an alpha helix.Many people in the audience witnessed a three-dimensional molecular model for the first time, and it was so grand.The model looked "lifelike," with individual atoms painted bright red, white and black neatly fitted together, twisting and bending around each other to form a thick, knurled column.In the spiral, the slightly stretched curves are clearly visible, and each atom is vivid; each part is different in shade, weight, and well-proportioned, and the visual effect displayed makes any other model pale in comparison.The chemical structure of Pauling's subjective imagination was vividly reflected, which attracted bursts of exclamation from the audience.At the end of his lecture, Pauling cited various evidences that this structure exists in many natural materials.Afterwards, professors and students of Caltech stepped forward to shake hands with Pauling, asked this and that, carefully inspected and stroked the spiral model. Lectures like those at the Kerkhoff Symposium were like rehearsals for a field tour, giving Pauling the opportunity to answer all kinds of questions before writing a detailed paper.However, he did not hear any substantive criticisms. It seems that everyone was very impressed.Pauling became more confident about the structure he envisioned, especially the alpha spiral. With growing self-confidence, Pauling and Corey spent the winter of 1950 and 1951 busy extending their gains to other proteins, such as collagen and feather uranium.Glue proteins, muscle proteins, etc., look for structures, many of which contain alpha helical components in their more complex structures.The cooperation between the two formed a fixed program: Pauling proposed the basic idea of ​​the structure, and Corey made this idea meticulously and carefully into a precise and perfect model.At times, the two talked about the rough spots, where Cory's work might reveal areas of weakness in Pauling's vision, and the two then worked together to further grease and polish those areas.In this way, one structure after another found its place, and news of its success spread like wildfire in the world.At Cavendish, researchers in the Prague group hadn't paid much attention to Pauling and Corey's previously obscure note in the Journal of the American Chemical Society, and they had been waiting for Pauling to publish a more detailed one. paper.While in New York, in February 1951, Weaver was eager to learn the details of this series of breakthroughs. He sent a Rockefeller Foundation official familiar with protein research to Pauling's laboratory. His name was Loomis. .The lab, Loomis found, was a place where bold ideas abounded. "There is no doubt that Pauling was a man of great imagination, ambition, and intelligence," Loomis wrote in his diary after spending only one day with Pauling. "However, he has gone off course in some cases (for example, 'artificial antibodies'), and many of his inspirational pictures, models, etc., may be largely figments of the imagination, and it is difficult to count them as Solid and sound scientific creation." broad prospects Off course!Pauling may be able to accept this argument.He was really trying his luck on some levels.What the Kotorz ​​data show is probably just a strange characteristic of artificial polypeptides; the reflection data of 5.1 Angstroms cannot be found in the experiment. This phenomenon may have nothing to do with real proteins. For Pauling X-ray reflectance tests on models of this kind never seem to yield such results.In this regard, Pauling is still unable to make a convincing explanation.Despite this difference, he was determined to move forward, and he was going to try his luck.And on this issue, the team in Prague will never act rashly.At Cavendish, they used the data methodically to construct models from the dots on the photographic plate.But in Pasadena, with poor X-ray facilities and fewer people working on crystallography, it was all about luck.They boldly played the game at the level Pauling picked.To analyze the molecular structure of proteins, the models used are tens of thousands of times more complex than those used by others, but the accuracy must reach one-tenth or one-hundredth of an angstrom.In the absence of reliable data as a backing, if it were someone else, they would definitely be as shy as Prague and would not dare to act rashly. However, Pauling is unique.Middle age is the time in life when many scientists, content to rest on the achievements of their youth, dabble in administration.Pauling, however, was more ambitious, more energetic, and more confident than ever. As it turns out, self-confidence is the deciding factor.Pauling believed in his knowledge of chemistry; he understood the ins and outs of the subject better than anyone else in the world.Of all the branches of chemistry, he knew best how atoms make up molecules.All he knew about chemistry told him that the alpha helix, as well as the other protein structures he had envisioned, were correct.These structures were built by them on sound principles; years of elaborate modeling had proved their abilities.Do you trust yourself—the strategies you use to solve macromolecular problems, the randomness you use to discover patterns and build models—or do you trust the speckles on the X-rays?He has freedom of choice.He finally chose to believe in himself. Information is indispensable to Pauling.Feeling more and more troubled politically, he had to reflect on some of his beliefs in that area; he was already faced with the choice: stick to his beliefs or bow before a commission of inquiry.He chose to stand firm — while still trying to avoid accusations of contempt of the investigation.Mastering the stick, but aiming for the yard.He was unwavering and confident in himself.He has a clear conscience.He has the upper hand in this game and has no intention of retreating at all.At the moment when he is about to uncover the mysteries of life, he will never back down. February 28, 1951, coincided with Pauling's 50th birthday.Pauling blew out the candles on a birthday cake his subordinates had baked for him, accepted well wishes from colleagues, and sent a manuscript of a paper to the Proceedings of the National Academy of Sciences.The title of this article is "Protein Structure: The Dihydro-Strand Helical Structure of Polypeptide Chains", and the authors are signed by Pauling, Corey, and Branson.This paper gives a complete and very detailed description of the structure of the alpha helix and the gamma helix. While waiting for the official publication of this paper, Pauling was extremely excited and his joy was beyond words. He would inevitably boast about the importance of this research work and the original significance of their results. "The structure of our predictions differs from others' results presented in the literature in that our results are very precise, while others' results are more or less vague," Pauling wrote in the days after he sent his paper. Said it to Weaver. 'Oh thinks that, in a sense, this result marks the final resolution of the problem of protein structure. "Weaver was also very happy that his support to Pauling in the past two decades was not in vain. Therefore, he immediately sent George Gray, a resident reporter and publisher of the Rockefeller Foundation, to Caltech for an interview, as the trustee of the Fund. Prepare a comprehensive report. Gray found Pauling to be an ideal author, a scientist who knew how to present his work in plain, colorful language. (“I can put myself in my shoes As an atom," Pauling said to him. "I asked myself, what would I do if I were a carbon atom or a sodium atom.") Weaver began to reconsider whether he should contribute to Caltech's chemistry and biology Several million dollars in funding. Before the paper was published, Pauling also wrote to Dennis Flanagan, editor of Scientific American magazine, saying that he and Corey had overcome the problem of protein structure, and at the same time He added: "In my opinion, this is the most important step in this field in the last 25 years, maybe the last 50 years. Flanagan quickly wrote back, asking for more detailed information about the "blockbuster", and also asked Pauling to write an article on protein structure for the journal. The first paper is nothing more than an introduction.It seemed that once the results on the alpha and gamma helixes were published and the problem was solved, it became clear that the other protein structure problems that had been lingering in his mind all began to fall into place.Along with Corey, he spent March working on several other papers on protein structure. "I'm so busy right now that I barely have time to keep my feet on the ground," Pauling wrote to a former student in mid-March. "Working continuously day and night, almost to the point of forgetting to sleep and eat." Counting from the early years of searching for chemical bonds twenty years ago, this is the most comfortable scientific research he has engaged in.For this achievement, even he himself was surprised. In early April, Pauling and Corey sent another set of papers to the Proceedings of the National Academy of Sciences.This is one of the most unusual sets of papers in the history of science in the 20th century.The group of seven papers dramatically takes up almost all of the May issue of the journal.These articles have made a detailed discussion of the sheet structure of proteins, found a new model for the rachis, and proposed new ideas about artificial polypeptides, globular proteins and muscle proteins.Most exciting for Pauling was finding what he called "a jaw-dropping structure" for collagen, an important protein in tendons.In collagen, he believed, three helices coiled around each other to form a single chord. Any scholar in the world who studies proteins will immediately realize the far-reaching significance of Pauling's research.These structures envisaged by Pauling are very complete and extremely detailed.This is a field of research in which phenomena have never been seen before, and now everything pops up all at once: like a scholar who spends his life doing some respectable research, and one day suddenly, Wonderful thinking is like a fountain, bearing fruitful results; it is also like a composer musician who composes seven symphonies in one breath in the same day. In England, Bragg had just read the papers and, as if bewitched, rushed into Alexander Todd's chemistry department office at Cambridge.Todd was a well-known organic chemist and an old friend of Pauling's.Todd had never seen this man named Lawrence Bragg at Cambridge University before.He immediately noticed the flushed face of the physicist, and also saw what he was holding in his hand-Pauling's paper. “I said to him how happy I was to see him in the chemistry department office and asked him what wind brought him here,” recalls Todd.Bragg was "in a kind of feverish state" wondering how one should choose between Pauling's spiral structure and his own earlier model.Todd had read Pauling's manuscript before, so he said bluntly that he must choose Pauling's result because the peptide chain in it has straight characteristics.Bragg claimed that the peptide chain could not be a planar chain. At this time, Todd introduced him to the knowledge about the resonance structure and the characteristics of multiple chains. "If you had checked with me before, I would have cleared up the situation for you," he said.Embarrassed, Bragg set off to return to the physics department. "I bet he didn't read The Nature of the Chemical Bond carefully," Pauling said triumphantly when he heard the trifle from Todd. Perutz used a Saturday morning to read all the papers co-written by Pauling and Corey in one go, and then he went straight into his laboratory.If the results of these scholars at the Caltech are correct, there should be 3.7 amino acids in each turn of the alpha helix, and the distance occupied by each amino acid in the direction of the chain length is 1.5 angstroms.On the protein backbone, the distance between such amino acid repeats should be shown on the X-ray diagram. However, the size of 1.5 angstroms is too small, so special experiments must be used to distinguish clearly.Still, it is worth doing the experiment, because of the many structures conceived for alpha keratin, only Pauling's helix would leave distinctive spots on photographic film; "fingerprint".Perutz placed a horsehair in his x-ray equipment and surrounded it with photographic film to photograph the expected reflections.He pressed the shutter.After the negative was developed, he immediately scanned the entire frame.That's right: just at the far edge of the photo, a blurry blob is seen.This reflection indicates the presence of a structural phenomenon that repeats every 1.5 angstroms.Perutz conducted an X-ray irradiation experiment on a porcupine quill, and also found this reflection phenomenon.He later did the same for artificial peptides and hemoglobin.He even found the spot on the far edge of an X-ray of the protein taken years ago, but they hadn't noticed it before.Perutz is an unusually unselfish scholar who takes pleasure in confirming someone else's work as if it were his own.他在给鲍林的信中写道：“这一预测得到证实、并在血红蛋白的试验中最终找到了有关的反射迹象，这是我毕生最最令人激动的发现。”随后，他发表了证实这些结果的具体资料，其结论是：“发生反射的间距是对其他各种模型的否定，但与鲍林、科里和布兰逊关于3.7个残基螺旋的理论是完全吻合的。”佩鲁茨还援引了帕萨迪纳研究小组得到的其他数据，他继续写道：“再也没有必要怀疑他们的结构是否正确了。” 到了6月，布拉格根据在自己的工场里得到的证据，承认阿尔法螺旋也许具有某种合理性——尽管用它仍然无法解释天然角蛋白为什么给出的是5.1埃的反射——他还致函祝贺鲍林的论文，特别是关于阿尔法螺旋的那篇论文，称此文开辟了“广阔的前景”。使鲍林感到非常欣慰的是，他的竞争对手写下了这样的话：“我认为，这是在认识蛋白质的过程中非常真实而又至关重要的进展，为此我衷心地向您表示最最热烈的祝贺。”但是，超越阿尔法螺旋的“广阔前景”到底是什么样子，此时尚没有定论，研究蛋白质的英国学术界开始一篇一篇深入细致地钻研鲍林撰写的其他论文。 错误百出，用心险恶 1951年上半年，鲍林在蛋白质结构的研究方面花费了大量的时间，相对来说，他过问政治的时间就很少了。然而，在那些以追查公众生活中赤色分子为业的人看来，这可算不了什么。在联邦调查局、特尼委员会和众议院非美活动调查委员会之间，情报是相互交换的，因此，鲍林已经成为内定的美国知名人士中，在每一个调查委员会的共党嫌疑分子名单上都是首当其冲的人物。在1951年这段时间里，每当提及科学界或和平运动中赤色颠复活动时，鲍林总是首先受到指摘和攻击的一个人。反共的通讯刊物《警惕》用了三期的篇幅向读者通报了鲍林在加州教育调查委员会出庭的情况，并且还不厌其烦地罗列了他公开露面的情况。 4月1日，也就是鲍林和科里寄出七篇有关蛋白质的论文供发表的那一天，众议院非美活动调查委员会点名指摘鲍林是“让美国放下武器和失败运动”中最活跃的美国人之一，因为他参加了一场虚伪的“共产党和平攻势”。在这一指控中并没有什么新鲜的东西——证据是已经公开的一份左翼团体的名单和鲍林参加活动的的记录——但是，这次攻击的火力更加猛烈了。“他的活动的全部记录……表明，莱纳斯·鲍林博士首先热衷于让许多团体利用他所取得的科学成就，这些团体都俯首贴耳地听从美国共产党和苏联的指挥”，众议院非美活动调查委员会发表的一份新闻公报这样说。“1946年以来，鲍林教授丝毫都没有偏离对共产主义事业的这种类型的忠诚。”为了回答这一类攻击，鲍林对记者说：“对于我所注意到的每一次和平运动，我在不同程度上都把自己看作为其中的一员，我将继续顺应自己的良心和吩咐竭尽自己的努力。” 这一指控在报纸上头版登出来以后若干天，鲍林打开了一封来自西弗吉尼亚马歇尔学院院长的来信，这位院长在信中表示遗憾地收回向鲍林发出的给有关领域科学家作一次讲演的邀请。这位院长写道，问题当然不在于鲍林的政治信仰，而是因为这可能引发当地公民的“强烈抗议”，从而有可能使鲍林夫妇陷于不必要的窘境。然而，鲍林却不买账。“您竟然使用这种方式行事，为此我深表不满，”他在信中这样回敬对方。他建议对方重发邀请，后来就再也没有收到对方的回音。 在跑林看来，更欠公正的当推夏威夷大学校务委员会委员们的行为了。他曾被安排为该校一幢新的化学大楼落成典礼剪彩，但是校务委员会受到该州反颠覆官员的警告。这些官员声称，他们从加利福尼亚的同行那里收到了特尼委员会关于鲍林的一份档案材料。于是，校务委员会迫使化学系撤回了对鲍林的邀请。鲍林是从一位记者那里得知这一消息的，他同样直言不讳地提出了自己的批评意见：“我非常吃惊，堂堂一所大学的校务委员会，本来应当是由一些志士仁人组成的，然而这个机构竟然可以不向对方指控就审判一个人，并公开宣布这个人有罪，而且根本就不给人家申诉的机会。”当这一争议公之于报端时，媒体派人找到杜布里奇了解他的意见，这位校长守口如瓶，只说他看不出这一问题与加州理工学院有什么相干。 静下心来以后，鲍林给夏威夷大学校务委员会去了一信，对他们的行为表示“强烈的愤慨”。“你们认为，一个美国人，坚持自己的独立主张，不愿受人支配，反对颐指气使的官员指手画脚。就成了非美国人了吗？”他这样写道。“我不这样看。我想，这种人与那些不表示反对态度的人相比，更加具有美国人的气质。”他随信还附上了一份有关自己政治信仰的声明——其中也提到他拒绝参加共产党一事——他要求对方重新发出邀请，并且暗示，要是对方不这样做，他将诉诸法律。但是，该校校务委员会仍然坚持自己的立场。 不管怎样，鲍林还是决定到这个群岛去走一趟。此时正值度假的美好时光。他的几篇关于蛋白质的论文刚刚刊出，政治气候也在升温，他需要休息一下了。况且，到夏威夷去也是表明自己鄙夷和不满的一种方式。“我想，到檀香山去还是值得的。到那里可作几次科学讲座，同时也可向这个群岛的居民表明，夏威夷大学校务委员会撤回对我的邀请是犯了多大的错误，”他在给朋友的一封信中这样写道。他说服了美国化学学会夏威夷分会邀请他作一系列讲演，于5月底带着爱娃·海伦一道飞到了檀香山。这次旅行终于成了一个非常令人高兴的转折点。每次讲演都受到一批批热情洋溢的科学家的热烈欢迎。大家都急切希望了解他的最新发现。讲演完毕后，许多人上前与鲍林握手，感谢他蔑视有关方面的狭隘偏见所显示出来的勇气。檀香山报界也站在鲍林一边，开始质问夏威夷大学校务委员会为什么采取那样的行径。 这对鲍林是一个很大的鼓舞。看来，在一段较短的时间里，由丁奋起坚持自己的信念，他不但维护了自己的声誉，而且给别人也带来了希望。 然而，从夏威夷归来后几个星期，气氛又变得沉闷起来。从1948年开始，鲍林曾多次成功地摆脱有关方面要他接受忠诚计划的审查，但是，要避开这种纠缠将会愈来愈困难。1951年，朝鲜战争烟火弥漫，罗森伯格审判案又再次将原子弹间谍问题变成了人们议论的中心。杜鲁门签署了另一项行政命令，进一步提高了忠诚的标准。只要对一个人的忠诚有疑问，那怕缺乏任何切实的证据，就可以成为免去这个人公务员职位的理由。成百上千个案例又重新开庭审理，爱德华德·康顿的案子就是其中之一。这一次，这位长期受难的物理学家吃足了苦头，最后被迫辞去了国家标准局局长的职务。 政府用于科学的经费，特别是用于属于保密防务研究的经费大大增加了。许多科学家、技术人员和工程师为了要找到工作，不得不接受有关方面对自己进行忠诚的鉴定。本来，只是军方对下属有关人员进行忠诚的鉴定和听证，但在此时，面对新近大量涌现出来的有关平民的案件，有关方面对审查制度作了相应的调整，许多非军方人员也要接受忠诚的鉴定。不过，在其冠冕堂皇言论的背后，忠诚鉴定实际上成了一项影子式的法律制度。非军方科学家如要得到一项属于某一密级的政府合同，那就必须将自己的档案资料送交地区司令官审阅。如果发现可疑的活动和联系，那么这个人的档案就要送到一个地区性人事安全部门作进一步的审查。那个安全部门有权撤销此人参与机密工作的许可——此人将不得参与任何保密项目的研究——而且还用不到召见当事人或者提供任何证据。科学家一旦被列入黑名单，唯一的求助手段是向就业资格审查委员会申诉。如果是第一次，当事人可以在律师的陪同下亲自陈述自己的情况。就业资格审查委员会举行的听证会，并非精确意义上的审理——而是在判决已经作出，并且由军方对平民的政治活动作出判断之后，在法律制度之外进行的一种活动——当然，听证会在形式上很像法庭审理，有审问、抗辩、律师等等。这是一种《阿丽丝漫游记》式的制度。就业资格审查委员会作出判决以后，当事人就再也无处可以申诉了，陪审团作出的是最终判决。 成千上万名学者受到这一荒唐制度的摆布。一个人一旦因故被排除在某一密级之外——其理由可以仅仅是参加过某一可疑的团体——那么，在别的地方，不管是不是政府项目，此人要找到饭碗将都是非常困难的。忠诚鉴定并没有查出任何原子弹间谍，但在实际上起到了堵住不同政见者之口的作用。五年以前，这种开列黑名单的基本做法，曾经有效地迫使电影界纳入安分守己的轨道，现在则被用来防止学者在政治上说三道四了。 此时，鲍林本人也被卷入了忠诚鉴定的浪潮。 鲍林曾避免涉足国防保密项目的研究。但是，根据合同规定，他是加州理工学院教职工委员会的成员之一，这一职位要求他审查其他人提交的从事保密项目要求资助的申请。空军要求，任何人阅读他们的有关合同，那怕此人具有审查人的身份，也都应当接受较低密级的资格审查。这种人只能接触属于“机要”级或“内部”级的材料，不能参阅“机密”级或“绝密”级的文件。对有关人作这种较低密级的鉴定，原本只是加盖橡皮图章的例行公事，很少要求本人到场接受就业资格审查委员会的全面审查。1951年初，加州理工学院将鲍林和另外一些校务委员和员工的名单上报，让有关方面作这种较低密级的资格鉴定。所有人都顺利过关——但鲍林除外。 7月下旬，鲍林收到了当地军事安全委员会的一封公函，正式通知他要求接触加州理工学院保密材料的申请不予批准。根据该委员会掌握的“情报”，“你曾是一名共产党员，一名与共产党员有密切联系的外围人员，……你还与信仰共产党意识形态的众多团体发生过密切的联系，或者就是其中一员，在许多场合，你曾公开为知名的共产党人和共产主义意识形态进行辩护。” 一切全是不实之辞。鲍林立即就上述指控向就业资格审查委员会提出申诉。听证会定于11月份举行。 颇具讽刺意味的是，就在鲍林在美国被指控为共产党人的同一时间里，有消息传到加州理工学院，称他受到了苏联化学家的严厉谴责，说他基于共振的化学结构理论“错误百出，用心险恶”。李森科时代的俄国学者为了吹嘘俄罗斯在结构化学方面取得的成就，用了两年的时间在与鲍林的“资产阶级反动”化学思想决裂，特别是要与他的并不真正独立存在的唯心主义共振结构的用法决裂。他们认为，共振理论与唯物主义唱反调，因而也是反苏的。1951年夏，苏联科学院化学部通过正式决议，认为鲍林的做法是“伪科学”，是“唯心主义”，因此必须摒弃。《真理报》大力鼓吹这一决议，并且在苏联的科学出版物上激起了一阵阵声讨的浪潮，称鲍林研究化学的方法是“臆想捏造出来的玩意，是与现实毫不相干的偷懒想法”。一位当代观察家在《美国化学教育期刊》上发表文章写道：“攻击辱骂之猛裂和粗暴，这在化学界是史无前例的。”自此开始，苏联化学走上了反鲍林的轨道。 鲍林现在处在这样一种奇特的地位：一方面，美国人辱骂他是共产党人；另一方面，苏联人又把他称为反动分子。在私下里，鲍林对俄国人的谩骂还是“颇为关注”的。他在给一位朋友的信中写道：“我真不明白这样一种攻击到底有多大意义，他们到底想干什么。”在公开场合，这倒提供了一个可以减轻破坏性后果的可能，杜布里奇就迫不及待地抓住了这一机会。当《纽约时报》的一位记者将俄国科学家通过的反鲍林决议电传到加州理工学院征求看法时，该院用了整整三页的新闻通讯作回答，强烈谴责李森科主义，并且强调了鲍林对共产主义科学的批评意见。“如果不容许俄国科学家应用共振理论，或者剥夺他们在其他方向上进行科学研究的自由，那么俄罗斯科学必将落在西方科学的后面，俄国的技术也会因此而受到损害，”该文引用鲍林的话这样说道。后来，《纽约时报》和《时代》杂志在报道中将鲍林描绘成了西方科学反对俄国人扼杀真理的一名卫士。 game rules 正当俄国人和美国人都在忙忙碌碌地清算鲍林的活动，试图找到他在政治上图谋不轨的行为时，布拉格、阿斯特贝里和其他英国学者却在细心地审阅他关于蛋白质研究的论文，以便发现其中的破绽。到了1951年秋天，他们自认为已经找到了大量错误。一方面，佩鲁茨证实了阿尔法螺旋的存在性，发现这种结构存在于许多种蛋白质中，具有1.5埃的阿尔法螺旋指纹；另一方面，他在羽轴蛋白质中却没有找到这一种结构，然而根据鲍林的预计应当是能够找到的。佩鲁茨得出结论说，鲍林和科里提议的羽毛结构是错误的。佩鲁茨还认为，鲍林曾设想，肌肉收缩模型可使片层结构收缩为阿尔法螺旋，这是不对的，因为无论在扩张形式还是在收缩形式中都找到了阿尔法类型存在的证据。伯纳尔曾打算接受纤维蛋白中存在阿尔法螺旋的理论，但他心里很清楚，这对他正在研究的核糖核酸酶和胰凝聚蛋白酶这两种球状蛋白质的结构并没有帮助。科托尔兹公司的研究组不同意鲍林关于人造多肽的尺寸所说的话。鲍林关于松散的枷玛螺旋的意见也受到了批评，因为在其中心存在着一个大洞，完全装得下一些细小的分子，因而会使其不稳定。最令鲍林失望的是，他为胶原蛋白设想的结构——三螺旋索结构，并没有得到英国Ｘ射线研究结果的证实，而他认为这种结构的发现为解释物质的抗拉伸特性做了一件好事。 1951年下半年，鲍林花了大量的时间考虑怎样回答这些批评，并且继续修正自己关于蛋白质结构的理论。他感到这一工作极重要，以至他谢绝了哈佛大学要他担任客座教授的邀请，目的是要集中精力攻克这一个堡垒。他还推迟了预先计划好去欧洲的一次旅行，同样是为了把自己的思路理得更加清楚些。羽毛中阿尔法螺旋的指纹可能是非常隐蔽的，因为他已注意到，各个螺旋具有不同的相位；肌肉可能包含着“非拉伸性阿尔法角蛋白”，它永远用阿尔法形式存在着。他澄清了科托尔兹公司研究组的一种误解；不久以后，该公司研究人员就承认，对他们研究的人造多肽来说，阿尔法螺旋是合理的。然而，对于伽玛螺旋的情况，鲍林打算放弃了，他对其稳定性向来就感到有些吃不准；到了秋天，他就完全将这个问题置于脑后了。鉴于愈来愈多的证据不利于他为胶原蛋白提出的结构，他又回复到了一个新的出发点。到1951年末，他终于认识到“我们提议的这种结构……不完全合理，我认为在总体上是正确的，但需要作些细小的修正”。与此同时，他与科里又想到两种片层结构，同时还考虑为某些蛋白质提出一种他们称之为“波层”的结构。 不过，在鲍林的阿尔法螺旋这一惊人的成就面前，人们提出的种种批评的意见也就黯然无光了。尽管阿斯特贝里不断提醒鲍林，应当对5.1埃这个数据得不到证实这一点作出明确的解释，但是鲍林提出的螺旋结构都有其充分的依据，这一点也是无可辩驳的事实。使人困惑不解的Ｘ光反射现象，看来是与基本结构本身无关的某一种因素造成的。鲍林在对阿尔法螺旋进行推广时，提出了各种各样的片层结构，看来也是很有道理的。在英国，人们开始认识到，尽管鲍林在其他结构问题上前进得快了些，但他终究解决了一个大问题，也即角蛋白的收缩形式和扩张形式的问题，阿斯特贝里相信，这种物质是所有蛋白质生成的源泉。正如鲍林在那时写下的那样，“我心里非常清楚，这些发现将会迎来蛋白质研究的一个新时代。” 事实也确是如此。鲍林对蛋白质的研究使这场竞争游戏的规则发生了变化。正是鲍林始终相信氢键是十分重要的。同样也是鲍林显示了根据精确的化学定律建造模型的巨大威力——这种随机研究的方法，使受过高等教育的人有可能利用猜测最终结果的办法，来解决复杂的Ｘ射线那样的问题。仍然是鲍林坚持将结构的精确度定到百分之一埃以内，从而将这场竞争提到这样高的水平，以至任何关于蛋白质结构的一般性粗糙的想法根本就没有立足之地。从此开始，人们提出任何一种蛋白质结构，都得满足鲍林对精度的要求。另外还有一点很重要，正是鲍林彻底打破了英国人有关整数对称性的思维定势。根据这种思维定势，人们一直认为晶图应具有对称的空间结构；正是因为这种思维定势，导致布拉格和佩鲁茨迷失了前进的方向。在阿尔法螺旋结构的理论提出以后，研究生物分子的晶体学家在思想上得到了解放，他们开始用新的方式思考生物分子，寻求其非整数特性——因而可以根据自己的想法弄清楚真实的研究对象了。 这是一项了不起的成就，鲍林确信自己是当之无愧的。1951年9月，来自42个国家的18000名化学家会集在纽约市，举行世界化学大会，又称纯粹化学和应用化学代表大会——这在历史上是最大的一次化学家聚会，庆祝美国化学学会成立如周年纪念日。会议规模宏大，地点又选在曼哈顿岛的中心，因此得到了新闻媒体的大量报道。鲍林根据大会的议程作了好几次报告，其中包括一次关于蛋白质结构的重要讲演。他还协助加州理工学院新闻系整理了一份长达六页的新闻稿，其中简要地阐述了他的发现所具的重大意义。这一篇文章后来成了科学家进行公关活动的一篇杰作。文章较为详细地概括了鲍林发现的成果，着重提到了在这些发现背后有关人员作出的努力，同时还强调了这些发现对科学和医学将会产生的巨大影响。文章使用的语言都是记者能够理解的，其中不乏诸如“生命的奥秘”那样一些引人注目的用语。美国化学学会公关部工作人员急切希望媒体能最大限度地报道大会的实况。除此之外，他们心里很清楚，鲍林这个人气度不凡，又平易近人，因此也乐于给鲍林的工作提供必要的帮助。 这样，鲍林在大会上出尽了风头。整个大会期间，他所作的关于蛋白质结构的讲演吸引的听众最多。这次讲演是安排在罗斯福宾馆的大会议厅中进行的。像往常一样，他兴致勃勃地面对着将大厅挤得水泄不通的听众，侃侃而谈。听众中不少人是来自几家大报的记者，另外还有一名来自《生活》杂志的摄影师。一切都非常顺利，事事都无可挑剔——一直到快要结束时，开始进入提问和答辩的阶段，一位头发稀疏、相貌一般、身着西服的男子从后排座位上站起，声称是他第一个发现了阿尔法螺旋。这个人就是莫里斯·哈金斯。这位科学家在1943年就曾提出蛋白质具有螺旋状结构，为此他曾要大家去寻找这种螺旋。这使鲍林一时感到很尴尬，他在头脑里苦苦思考着，试图回忆起哈金斯研究所得的详细结果。然后，他终于回过神来，指出哈金斯关于螺旋形态的基本思想是正确的，但他和布拉格一样，没有认识到平面肽基的必要性和非整数类型的重要性。但是，这并没有平息哈金斯显示出来的怒气。哈金斯和鲍林的交往可以追溯到很久以前——早在20年代，他曾用有关化学键的某些早期的想法帮助过鲍林，而且也提出过氢键的想法——但是，在每一种场合，一直是鲍林出名得利，相形之下，哈金斯的业绩却再三地受到冷落，他不想让鲍林在蛋白质研究方面窃取他的思想。鲍林花了好几个星期的时间试图说服他，他的模型相对来说比较含糊，在某些重要方面甚至是错误的。 这短暂的口头交火，不但没有使在场记者对鲍林的成果产生怀疑，正好相反，他们对这些发现的重大意义留下了更为深刻的印象。第二天，《纽约时报》的大幅标题是：“化学家揭开蛋白质奥秘——战胜疾病的有力帮手——探索生命起源道路上第一座里程碑——有可能解开千古之谜。”随附的报道使用了发动总攻击令式的语言，将这一发现比拟为“攻克自然界重要堡垒的第一个重大的据点——细胞质的结构，也即生命的物质基础——这一堡垒在不久以前还一直是坚不可摧的。”消息很快地传遍了全国。两个星期以后，五百万读者在打开《生活》杂志时，看到了鲍林的巨幅照片。照片上，他笑容可掬，手指着他填补空间的阿尔法螺旋的模型，标题是“化学家解开大秘密”。他在蛋白质结构问题上取得的成就，使他进入了世界上最著名科学家的行列。 就业资格审查委员会 两个月以后，鲍林被召到就业资格审查委员会面前，他又得为自己的名誉而战了。 无论在公开的场合，还是在杜布里奇收到的一系列信件中，鲍林的政治立场都不断地受到来自右翼的攻击。杜布里奇明白，大多数保守派人士，在一些情况下还有一些非常有钱的客人，他们是学校的经济后盾。这些人不喜欢鲍林，这一情况正在使学校失去巨额的资助。在那年10月份联邦调查局的一份报告中，杜布里奇和加州理工学院的许多人对鲍林的态度是这样归纳出来的：“在加州理工学院的员工中，谁也不相信鲍林真的是共产党员，大家将他划归为有点（原文如此）爱出风头的人。许多人指出，鲍林经常想看到自己的名字在报纸上出现，这种情况已经给加州理工学院带来了许多麻烦的事。”这位特工又写道：“鲍林近来名声不佳，加州理工学院校方对此感到很不快，这在全校的一般员工中也有所反映。……（此处原文已涂没）觉得他是一位独一无二的科学家，但也开始相信，迟早有必要采取某种措施，因为这已使学校失去了可能得到的几百万美元捐款。”于是，尽管杜布里奇在公开的场合仍一如继往地保护鲍林，但在私下里却再三劝说鲍林降低一下活动的调门。 在为就业资格审查委员会听证会作准备的过程中，杜布里奇在鲍林问题上的两面性做法得到了充分的体现。鲍林曾要求杜布里奇为自己指派一名律师，但这位加州理工学院的校长拖延了很长的时间不答复，致使鲍林失去了希望。他感到最好还是雇一名自己信得过的人。此人就是本地的美国公民自由协会激进分子阿伯拉罕·林肯·威林。鲍林一家人是在第二次世界大战期间抗击日冠歇斯底里的斗争中认识威林的。从那时起，威林就在公众心目中赢得强硬异常的激进律师这一名声，他随时准备和各种各样的调查委员会对着干。在非美活动调查委员会的一次听证会上，威林因为不肯闭口而被警卫人员驾着扔出了法庭，他也因此而远近闻名了。就在鲍林案听证会举行前的星期四，杜布里奇召见鲍林，告诉他威林不能当他的辩护律师，并且为他提供了另一位人选。鲍林回答说，时间太晚了。“我将尽力代表学校和我本人，让大家满意，威林先生也会这样做，对此我抱有信心，”他这样说道。鲍林还建议杜布里奇雇一名律师在听证会上代表加州理工学院作辩护。 星期一，鲍林走进了洛杉矶联邦大厦810房间，后面跟着威林和他们两人选中的一批鲍林品行的见证人。鲍林面对着陪审团就坐。听证会刚宣布开始，鲍林就宣读了一份长达十三页的声明，全面总结了自己的生活经历和政治信仰。他向陪审团成员谈到，他的园丁是一位美籍日本人，他们两人在一起相处，使他看清了一些社会问题的实质。通过阅读报纸和对历史的研究，他逐渐形成了一套自己特有的政治见解。“我没有对任何一个政党或团体作过任何一类承诺，”他对陪审团说。“我从来就不是共产党人，现在也不是共产党人。我与共产党从来就未发生过牵连。” 鲍林说，他是一个美国人。实行典型的民主制度，维护各个国家和民族之间的和平，尊重美国宪法中规定的人权，承认最高的道德准则，这些就是他信仰的准则。接下去，他又简要地说明了自己为政治活动付出的代价。他告诉陪审团，他为此失去了伊莱·莉莉公司顾问的资格。“我目前的雇主，也就是加州理工学院，为了迫使我停止政治活动，对我施加了巨大的压力。”他在声明的末尾，用了很大的篇幅回顾了他为国家所做的大量工作。他曾赢得杜鲁门总统颁发的奖章。他对自己作为一名科学家所掌握的知识作了非常自信的评价——“我认为，就总体上来说，我所掌握的科学知识，比任何一个美国人都更为广博——数学，物理学，化学，生物学，还有地质学（矿物学），”他说道。他申诉自己是清白无辜的。“我知道，由于我的政治活动和社会交往，有人在用于鉴定的分级档案里将我列入了不可靠一类，”他对陪审团说。“我本人认为，考虑到本人的人格和品德，考虑到我对国家可能提供的服务，考虑到我的人生价值，应当把清白的名声还给我。” 在洛杉矶，就业资格审查委员会花了两天的时间，例行公事般地对鲍林进行了令人乏味的盘问，并且出示了一份常见的清单，上面列出了“可疑”团体的名称、发言稿和一些经过签署的文件。唯一逗人发笑的是，陪审团顾问竟然问了这样一个问题：“你到底是还是不是保护红木组织的成员？”鲍林禁不住朗声大笑起来。最后，在听取品行见证人的不着边际的证词后，陪审团决定12月初在华盛顿继续举行听证会。这称得上大案——鲍林是至今面对就业资格审查委员会的一个最为有名的科学家——而且他们也不急于收场。 但是，华盛顿听证会后来根本就没有举行。洛杉矶听证会结束后第二天，杜布里奇给鲍林发出了一封令人吃惊的信函。他在信中称，学校人事处已对有碍于鲍林要求恢复名誉的一次工作上的“疏忽”作出了处理。看来，鲍林之所以要接受就业资格审查委员会的听证会审查，原因就在于他的名字“因误解”而被列入要求参阅绝密级文件的科学家名单，这些科学家正在从事名为“远景工程”的一个氢弹项目的研究。原来这一切全都是误会，就业资格审查委员会对他作了错误的调查。杜布里奇嘱咐校人事处的主管写了一封“道歉信”。鲍林将这封信转交给在华盛顿的就业资格审查委员会，之后，整个案子就被取消了。 鲍林已深受其害。一方面，就像他以前受到加州教育委员会纠缠那样，他必须面对当地一批反共政客的鼓噪；另一方面，他从事国家级科学研究的资格也受到了威胁。由于失去了接触机密材料的资格，他作为加州理工学院的一名高级管理人员，有效地进行工作的能力就大打折扣了。举例来说，他不再有资格审核他手下的员工所提出的各种级别的资助申请。这种情况不但使他在学校里所处的地位发生了动摇，而且杜布里奇和其他反对他的后台老板很可能因此得出结论，应当削弱他的某些职权，甚至将他降级使用。事情已经非常清楚，鲍林的政治活动正在严重地影响到他作为创造性很强的一名科学家发挥自己的才能。 在此之前，鲍林一向在服从上级和独立思考之间，在讨人喜欢和坚持真理之间，小心翼翼地保持着平衡。就业资格审查委员会的听证会进入高潮，这种平衡状态也开始动摇。此时，他已清醒地认识到，在政治上与可疑的团体搞在一起，可能招来很多麻烦，还是小心谨慎为妙。 鲍林与爱娃·海伦进行了一次长谈，他打算后退一步了。 在杜布里奇发现人事工作出错后的几天时间里，鲍林向国家艺术、科学和专业人士委员会以及美国科学工作者协会寄去了辞职信。这两个组织当时正处于受人攻击的状态，被指摘为受到共产党的操纵。鲍林还对美国和平十字军运动