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Indian Journal of Biochemistry and Biophysics (IJBB) >
IJBB Vol.49 [2012] >
IJBB Vol.49(1) [February 2012] >
| Title: | Residual ordered structure in denatured proteins and the problem of protein folding |
| Authors: | Basharov, Mahmud A |
| Keywords: | Protein Folding
Protein Residual Structure
Protein Denaturation |
| Issue Date: | Feb-2012 |
| Publisher: | NISCAIR-CSIR, India |
| Abstract: | Structural 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. |
| Page(s): | 7-17 |
| CC License: |  CC Attribution-Noncommercial-No Derivative Works 2.5 India |
| ISSN: | 0975-0959 (Online); 0301-1208 (Print) |
| Source: | IJBB Vol.49(1) [February 2012]
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