Open AccessFolding of Polypeptide Chains in Proteins: A Proposed Mechanism for Folding
Author(s) -
Peter N. Lewis,
Frank A. Momany,
Harold A. Scheraga
Publication year - 1971
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.68.9.2293
Subject(s) - folding (dsp implementation) , protein folding , chain (unit) , mechanism (biology) , polypeptide chain , basis (linear algebra) , protein structure , range (aeronautics) , chemistry , beta (programming language) , amino acid , biophysics , computational biology , crystallography , physics , computer science , biology , biochemistry , materials science , mathematics , geometry , quantum mechanics , astronomy , electrical engineering , composite material , engineering , programming language
A mechanism is proposed for the folding of protein chains. On the basis of short-range interactions, certain aminoacid sequences have a high propensity to be, say, alpha-helical. However, these short helical (or other ordered) regions can be stabilized only by long-range interactions arising from the proximity of two such ordered regions. These regions are brought near each other by the directing influence of certain other aminoacid sequences that have a high probability of forming beta-bends or variants thereof, also on the basis of short-range interactions. An analysis is made of the tendency of various amino acids to occur in beta-bends, and it is possible to predict the regions of a chain in which a beta-bend will occur with a high degree of reliability.
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