Book Chapter10.1016/S0065-3233(08)60413-1
Experimental and theoretical aspects of protein folding.
Anfinsen Cb,Harold A. Scheraga +1 more
990
TL;DR: The development of conformational energy calculation procedures will enable the three-dimensional structure of a native protein to be predicted from the knowledge of its amino acid sequence and its interactions with the solvent in which it is dissolved.
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Abstract: Publisher Summary In the proper environment, a polypeptide chain can fold spontaneously to the three-dimensional structure of a native protein, and despite the possible presence of barriers in conformational space, the chain can find its way around these barriers to reach the structure of lowest free energy. This chapter describes the spontaneous folding of proteins; in vitro complementation of protein fragments; flexibility of proteins in solution: effect of cross-links and ligands, synthetic analogs of proteins; experimental approaches to the study of conformation; and energetic factors determining protein folding. The interatomic interactions within the chain and between the chain and the solvent dictate the folding and the range of the forces involved, is such that near-neighbor interactions are dominant. Folding is envisaged as taking place by the formation of nucleation sites in various parts of the chain, in response to near-neighbor interactions; the various nucleation sites become stabilized, when they are brought into proximity, so that long-range interactions can become operative. However, the development of conformational energy calculation procedures will enable the three-dimensional structure of a native protein to be predicted from the knowledge of its amino acid sequence and its interactions with the solvent in which it is dissolved.
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TL;DR: There is now a testable explanation for how a protein can fold so quickly: A protein solves its large global optimization problem as a series of smaller local optimization problems, growing and assembling the native structure from peptide fragments, local structures first.
References
Principles of Polymer Chemistry.
TL;DR: A good introduction to the history of the POLYMER CHEMISTRY can be found in this paper, where the authors present a good overview of the history and history of their work.
15.1K
Principles that Govern the Folding of Protein Chains
TL;DR: Anfinsen as discussed by the authors provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the Thermodynamic Hypothesis, and outlined potential avenues of current and future scientific exploration.
7.2K
The interpretation of protein structures: estimation of static accessibility.
B. Lee,Frederic M. Richards +1 more
TL;DR: The accessibility of atoms in the twenty common amino acids in model tripeptides of the type Ala-X-Ala are given for defined conformation and the larger non-polar amino acids tend to be more “buried” in the native form of all three proteins.
6K
Some factors in the interpretation of protein denaturation.
TL;DR: The chapter reviews that the denaturation is a process in which the spatial arrangement of the polypeptide chains within the molecule is changed from that typical of the native protein to a more disordered arrangement.
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Studies on the Principles That Govern the Folding of Protein Chains
Christian B. Anfinsen
- 01 Jan 1973
TL;DR: In his Nobel Lecture, Anfinsen provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the "Thermodynamic Hypothesis," and outlined potential avenues of current and future scientific exploration.