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• W2017162722 startingPage "596" @default.
• W2017162722 abstract "The process of formation of a globular structure by a long molecular chain has been examined. In this process, various regions of the chain interact with one another. We classify the contacts thus formed as “correct” and “erroneous” ones. The correct contacts are those characteristic of the final native globular structure. All other contacts can be treated as erroneous. It is demonstrated that globule formation may proceed actually without formation and subsequent decay of erroneous contacts. Our model permits avoiding examination of numerous erroneous variants inasmuch as the regions of the chain that form correct contacts enter “long-range” interactions that at the same time can be highly selective. The existence of interactions of this kind facilitates the mutual approach and interaction of just those regions of the chain that yield correct contacts. Based on database analysis, it is shown that the model is valid not only for abstract structures but also for real polypeptide chains capable of forming protein globules and helical fibrils." @default.
• W2017162722 created "2016-06-24" @default.
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• W2017162722 date "2011-08-01" @default.
• W2017162722 modified "2023-10-07" @default.
• W2017162722 title "On the optimal folding of protein molecules" @default.
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• W2017162722 doi "https://doi.org/10.1134/s0006350911040166" @default.
• W2017162722 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21950060" @default.
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