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General theory of the long-range interactions in protein folding
Authors:V.A. Namiot  A.V. BatyanovskiiI.V. Filatov  V.G. TumanyanN.G. Esipova
Affiliation:a Skobeltsyn Institute of Nuclear Physics of M.V. Lomonosov Moscow State University, 1(2), Leninskie gory, GSP-1, Moscow 119991, Russian Federation
b Institute of Biophysics and Cell Engineering of The National Academy of Sciences of Belarus, 27 Akademicheskaya street, Minsk BY-220072, Belarus
c Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences, 32 Vavilov street, Moscow 119991, Russian Federation
Abstract:The process of the globular structure formation from a long molecular chain is examined in a general sense. In the course of this process various regions of the chain interact with each other. The bonds formed during this process are classified as native and non-native ones. Native bonds are formed in native globular structure. All other bonds are “incorrect” (non-native). It is demonstrated that the globule formation can occur actually without production and subsequent decay of non-native contacts. The proposed model allows to avoid a search of numerous non-native variants since long-distance interactions with a high selectivity take place between the chain regions that form native bonds. The presence of these interactions prompts the chain regions which yield native contacts start to draw together and to interact. The databank data analysis shows that the developed model can be applied not only to the abstract structures but also to real polypeptide chains which are able to form both globular structures and helical fibrils.
Keywords:Protein folding   Long-distance interactions   Selectivity   Quick search of a native state
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