Residual ordered structure in denatured proteins and the problem of protein folding.

dc.contributor.authorBasharov, Mahmud A
dc.date.accessioned2012-08-09T10:41:45Z
dc.date.available2012-08-09T10:41:45Z
dc.date.issued2012-02
dc.description.abstractStructural characteristics of numerous globular proteins in the denatured state have been reviewed using literature data. Recent more precise experiments show that in contrast to the conventional standpoint, proteins under strongly denaturing conditions do not unfold completely and adopt a random coil state, but contain significant residual ordered structure. These results cast doubt on the basis of the conventional approach representing the process of protein folding as a spontaneous transition of a polypeptide chain from the random coil state to the unique globular structure. The denaturation of proteins is explained in terms of the physical properties of proteins such as stability, conformational change, elasticity, irreversible denaturation, etc. The spontaneous renaturation of some denatured proteins most probably is merely the manifestation of the physical properties (e.g., the elasticity) of the proteins per se, caused by the residual structure present in the denatured state. The pieces of the ordered structure might be the centers of the initiation of renaturation, where the restoration of the initial native conformation of denatured proteins begins. Studies on the denaturation of proteins hardly clarify how the proteins fold into the native conformation during the successive residue-by-residue elongation of the polypeptide chain on the ribosome.en_US
dc.identifier.citationBasharov Mahmud A. Residual ordered structure in denatured proteins and the problem of protein folding. Indian Journal of Biochemistry & Biophysics. 2012 Feb; 49(1): 7-17.en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/140213
dc.language.isoenen_US
dc.source.urihttps://nopr.niscair.res.in/handle/123456789/13586en_US
dc.subjectProtein Foldingen_US
dc.subjectProtein Residual Structureen_US
dc.subjectProtein Denaturationen_US
dc.subject.meshElasticity
dc.subject.meshProtein Conformation
dc.subject.meshProtein Denaturation
dc.subject.meshProtein Folding
dc.subject.meshProteins --chemistry
dc.titleResidual ordered structure in denatured proteins and the problem of protein folding.en_US
dc.typeArticleen_US
Files
Original bundle
Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
ijbb2012v49n1p7.pdf
Size:
117.85 KB
Format:
Adobe Portable Document Format
Description:
Journal article
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.71 KB
Format:
Item-specific license agreed upon to submission
Description: