title: [Two mechanisms of protein folding: theoretical analysis].
abstract: In the present study, two possible mechanisms of protein folding are analized. One of them is based on the hypothesis that at the first step of protein folding a nucleus is formed and then the remaining part of the molecule or domain is folded around it. For example, β-proteins containing 3β-corners can fold in this way. According to the other mechanism, the three-dimensional structure of proteins is formed as a result of interactions between "ready-made" building blocks. Analysis of structural features of the 3β-corners and features of their amino asid sequences enable us to conclude that the 3β-corner can fold into its unique structure per se and can act as a nucleus or "ready-made" building block in protein folding. The larger protein structures can be obtained by stepwise addition of β-strands to the 3β-corner in accordance with a restricted set of rules as shown in the corresponding structural tree, which is available at http://strees.protres.ru/. On the other hand, complementary interactions of the two 3β-corners can result in formation of the fold that is observed in the serine protease domain and similar proteins.
authors.forename: A V
authors.initials: AV
authors.lastname: Efimov
authors.forename: E A
authors.initials: EA
authors.lastname: Boshkova
mesh_terms: D000596:Amino Acids / Q000737:chemistry / Q000235:genetics; D008962:Models, Theoretical; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D057057:Serine Proteases / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D057057:Serine Proteases