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How does protein synthesis give rise to the 3D‐structure?
Author(s) -
Ptitsyn O.B.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80799-9
Subject(s) - protein folding , kinetic energy , molten globule , maxima and minima , native state , folding (dsp implementation) , protein structure , statistical physics , chemistry , biological system , physics , chemical physics , crystallography , mathematics , biology , classical mechanics , biochemistry , engineering , mathematical analysis , electrical engineering
The recent experimental data on stages and kinetic intermediates in protein folding are reviewed. It is emphasized that these data are consistent with the ‘framework model’ proposed by the author in 1973. The model implies that protein folds by stage mechanism (secondary structure — molten globule state — native state) in such a way that the results of previous stages are not reconsidered in subsequent ones. Arguments are presented that both these hypotheses and available experimental data do not contradict the assumption that native structures of at least small proteins are nevertheless under thermodynamic rather than kinetic control, i.e. correspond to global minima of free energy.