TY - JOUR
T1 - Methinks it is like a folding curve
AU - Srinivasan, Rajgopal
AU - Rose, George D.
N1 - Funding Information:
This work was supported by grants from the NIH and the Mathers foundation.
PY - 2002/12/10
Y1 - 2002/12/10
N2 - Most often, the unfolded state of peptides and proteins has been modeled as a statistical random coil. Here, we suggest an alternative model based on the presence of a significant, temperature-dependent conformational bias in the unfolded population. Conformational bias is suggested by our calculations [Proc. Natl. Acad. Sci. USA 96 (1999) 14258-14263], and it is found in recent studies of both proteins and peptides. The imposition of even a modest bias would transform our assessment of the folding problem.
AB - Most often, the unfolded state of peptides and proteins has been modeled as a statistical random coil. Here, we suggest an alternative model based on the presence of a significant, temperature-dependent conformational bias in the unfolded population. Conformational bias is suggested by our calculations [Proc. Natl. Acad. Sci. USA 96 (1999) 14258-14263], and it is found in recent studies of both proteins and peptides. The imposition of even a modest bias would transform our assessment of the folding problem.
KW - Conformational entropy
KW - Protein folding
KW - Random coil
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U2 - 10.1016/S0301-4622(02)00147-3
DO - 10.1016/S0301-4622(02)00147-3
M3 - Article
C2 - 12487998
AN - SCOPUS:0037058965
SN - 0301-4622
VL - 101-102
SP - 167
EP - 171
JO - Biophysical Chemistry
JF - Biophysical Chemistry
ER -