Methinks it is like a folding curve

Rajgopal Srinivasan; George D. Rose

doi:10.1016/S0301-4622(02)00147-3

Methinks it is like a folding curve

Rajgopal Srinivasan, George D. Rose

School of Medicine

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	167-171
Number of pages	5
Journal	Biophysical Chemistry
Volume	101-102
DOIs	https://doi.org/10.1016/S0301-4622(02)00147-3
State	Published - Dec 10 2002

Keywords

Conformational entropy
Protein folding
Random coil

ASJC Scopus subject areas

Biophysics
Biochemistry
Organic Chemistry

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10.1016/S0301-4622(02)00147-3

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abstract = "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.",

keywords = "Conformational entropy, Protein folding, Random coil",

author = "Rajgopal Srinivasan and Rose, {George D.}",

note = "Funding Information: This work was supported by grants from the NIH and the Mathers foundation.",

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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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SN - 0301-4622

VL - 101-102

SP - 167

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JO - Biophysical Chemistry

JF - Biophysical Chemistry

ER -

Methinks it is like a folding curve

Abstract

Keywords

ASJC Scopus subject areas

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