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Principles That Govern the Folding of Protein Chains Author(S): Christian B

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Principles That Govern the Folding of Protein Chains Author(S): Christian B Principles that Govern the Folding of Protein Chains Author(s): Christian B. Anfinsen Source: Science, New Series, Vol. 181, No. 4096 (Jul. 20, 1973), pp. 223-230 Published by: American Association for the Advancement of Science Stable URL: http://www.jstor.org/stable/1736447 . Accessed: 16/10/2011 12:23 Your use of the JSTOR archive indicates your acceptance of the Terms & Conditions of Use, available at . http://www.jstor.org/page/info/about/policies/terms.jsp JSTOR is a not-for-profit service that helps scholars, researchers, and students discover, use, and build upon a wide range of content in a trusted digital archive. We use information technology and tools to increase productivity and facilitate new forms of scholarship. For more information about JSTOR, please contact [email protected]. American Association for the Advancement of Science is collaborating with JSTOR to digitize, preserve and extend access to Science. http://www.jstor.org 20 July 1973, Volume 181, Number 4096 ;CIENCE exists under conditions similar to those for which it was selected-the so-called physiological state. After several years of study on the ribonuclease molecule it became clear Principles that Govern the to us, and to many others in the field of protein conformation, that proteins of Protein Chains devoid of restrictive disulfide bonds or Folding other covalent cross-linkages would make more convenient models for the Christian B. Anfinsen study of the thermodynamicand kinetic aspects of the nucleation, and subse- quent pathways, of polypeptide chain folding. Much of what I will review deals with studies on the flexible and The telegram that I received from eight sulfhydryl groups to form four convenient staphylococcal nuclease the SwedishRoyal Academy of Sciences disulfide linkages take place.The origi- molecule, but I will first summarize specifically cites "... studies on ribo- nal observationsthat led to this conclu- some of the older background experi- nuclease, in particular the relationship sion were made together with my col- ments on bovine pancreaticribonuclease between the amino acid sequence and leagues Michael Sela and ]Fred White itself. the biologically active conformation. in 1956-1957 (3). These vvere, in ac- ..." The work that my colleagues and tuality, the beginnings of a long series I have carried out on the nature of of studies that rather vaguely aimed at Support for the the process that controls the folding of the eventual total synthesis of the pro- 'Thermodynamic Hypothesis" polypeptide chains into the unique tein. As we all know, Gutte and Merri- three-dimensionalstructures of proteins field (4) at the Rockefellrer Institute, An experiment that gave us a partic- was, indeed, strongly influenced by ob- and Ralph Hirschmanand his colleagues ular satisfaction in connection with servationson the ribonucleasemolecule. at the Merck Research Institute (5), the translation of information in the Many others, including Anson and have now accomplished this monumen- linear amino acid sequence into native Mirsky (1) in the 1930's and Lumry tal task. conformation involved the rearrange- and Eyring (2) in the 1950's, had ob- The studies on the renatturation of ment of so-called "scrambled"ribonu- served and discussed the reversibilityof fully denatured ribonucleaqse required clease (8). When the fully reduced pro- denaturationof proteins. However, the many supporting investigations (6-8) tein, with eight SH groups, is allowed to true elegance of this consequence of to establish,finally, the gene:rality which reoxidize under denaturing conditions natural selection was dramatized by we have occasionally called (9) the such as exist in a solution of 8 molar the ribonucleasework, since the refold- "thermodynamichypothesis " This hy- urea, a mixture of products is obtained ing of this molecule, after full denatura- pothesis states that the three-dimen- containing many or all of the possible tion by reductive cleavage of its four sional structure of a native3 protein in 105 isomeric disulfide bonded forms disulfide bonds (Fig. 1), required that its normal physiological miliieu (solvent, (schematicallyshown at the bottom right only 1 of the 105 possible pairings of pH, ionic strength, presencce of other of Fig. 2). This mixture is essentially components such as metal icons or pros- inactive-having on the order of 1 per- Copyright ? 1973 by the Nobel Foundation. thetic groups, temperature,and other) cent the activity of the native enzyme. The author is chief of the Laboratory of is the one in which the Gibbs free If the urea is removed and the Chemical Biology, National Institute of Arthritis, Metabolic and Digestive Diseases, National Insti- energy of the whole systenn is lowest; "scrambled" protein is exposed to a tutes of Health, Bethesda, Maryland 20014. This that that the native conformation is article is the lecture he delivered in Stockholm, is, small amount of a sulfhydryl group- Sweden, on 11 December 1972 when he received determined by the totalityr of inter- containing reagent such as mercapto- the Nobel Prize for Chemistry, a prize he shared with Stanford Moore and William H. Stein. It atomic interactions and hence by the ethanol, disulfide interchange takes is published here with the permission of the amino acid in a venenviron- and the mixture Nobel Foundation and will also be included in sequence, giv place, eventually is the complete volume of Les Prix Nobel en 1972 ment. In terms of naturaal selection converted into a homogeneous product, as well as in the series Nobel Lectures (in Eng- the of macJromolecules from lish) published by the Elsevier Publishing Com- through "design" indistinguishable native ribonu- pany, Amsterdam and New York. Dr. Moore's during evolution, this idea emphasized clease. This process is driven entirely and Dr. Stein's combined lecture appeared as a the fact that a single article in the 4 May issue of Science, page protein mo'lecule only by the free energy of conformationthat 458. makes stable, structural senise when it is gained in going to the stable, native 20 JULY 1973 223 structure. These experiments, inciden- discrepancy in rates would not have can be achieved. Model studies on tally, also make unlikely a process of been observed in the case of the fold- ribonucleasederivatives had shown that, obligatory, progressive folding during ing of structures that were not cross- when the intactness of the genetic mes- the elongation of the polypeptidechain, linked and, as discussed below, such sage representedby the linear sequence during biosynthesis, from the NH2- to motile proteins as staphylococcal nu- of the protein was tampered with by the COOH-terminus.The "scrambled" clease or myoglobin can undergo virtu- certain cleavages of the chain, or by protein appears to be essentially devoid ally complete renaturationin a few sec- deletions of amino acids at various of the various aspects of structuralregu- onds or less. points, the added disulfide interchange larity that characterizethe native mole- The disulfide interchange enzyme enzyme, in the course of its "probing," cule. subsequentlyserved as a useful tool for discovered this situation of thermody- A disturbingfactor in the kinetics of the examination of the thermodynamic namic instabilityand caused the random the process of renaturationof reduced stability of disulfide-bonded protein reshufflingof disulfide bonds with the ribonuclease,or of the "unscrambling" structures. This enzyme, having a mo- formation of an inactive cross-linked experiments described above, was the lecular weight of 42,000 and containing network of chains and chain fragments slowness of these processes, frequently three half-cystineresidues, one of which [see, for example (13)]. With two natur- hours in duration(7). It had been estab- must be in the SH form for activity ally occurring proteins, insulin and lished that the time required to syn- (12), appears to carry out its rearrang- chymotrypsin, the interchange enzyme thesize the chain of a protein like ing activities on a purely random basis. did, indeed, induce such a randomizing ribonuclease, containing 124 amino Thus, a protein whose disulfide Ibonds phenomenon (14). Chymotrypsin,con- acid residues, in the tissues of a higher have been deliberately broken and re- taining three disulfide-bondedchains, is organism would be approximately 2 formed in an incorrect way, need only known to be derived from a single- minutes (10). The discrepancybetween be exposed to the enzyme (with its es- chained precursor, chymotrypsinogen, the in vitro and in vivo rates led to the sential half-cystine residue in the pre- by excision of two internal bits of se- discovery of an enzyme system in the reduced, sulfhydryl form) and inter- quence. The elegant studies of Steiner endoplasmicreticulum of cells (particu- change of disulfide bonds occurs until and his colleagues subsequentlyshowed larly in those concerned with the secre- the native form of the protein substrate that insulin was also derived from a tion of extracellular, disulfide-bonded is reached. Presumably,disulfide bonds single-chained precursor, proinsulin proteins) which catalyzes the disulfide occupying solvent-exposed, or other (Fig. 3), which is converted to interchange reaction and which, when thermodynamically unfavorable posi- the two-chained form, in which added to solutions of reduced ribonu- tions, are constantly probed and pro- we normally find the active hor- clease or to protein containingrandom- gressively replaced by more favorable mone, by removal of a
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