Conformation of the backbone in unfolded proteins

Zhengshuang Shi; Kang Chen; Zhigang Liu; Neville R. Kallenbach

doi:10.1021/cr040433a

Conformation of the backbone in unfolded proteins

Zhengshuang Shi, Kang Chen, Zhigang Liu, Neville R. Kallenbach

Chemistry

Research output: Contribution to journal › Review article › peer-review

Abstract

Random coil has a long history of interpreting experimental results on unfolded proteins, in particular those from hydrodynamic and SAXS measurements of the radius of gyration (R_g). However, the model is inconsistent with older observations from Krimm's group as well as a wealth of spectroscopic techniques that demonstrate the presence of well-defined backbone structure within the unfolded states of proteins and peptides. This now puts into question prevailing views of unfolded proteins and alternatives must now be sought.

Original language	English (US)
Pages (from-to)	1877-1897
Number of pages	21
Journal	Chemical reviews
Volume	106
Issue number	5
DOIs	https://doi.org/10.1021/cr040433a
State	Published - May 2006

ASJC Scopus subject areas

General Chemistry

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10.1021/cr040433a

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title = "Conformation of the backbone in unfolded proteins",

abstract = "Random coil has a long history of interpreting experimental results on unfolded proteins, in particular those from hydrodynamic and SAXS measurements of the radius of gyration (Rg). However, the model is inconsistent with older observations from Krimm's group as well as a wealth of spectroscopic techniques that demonstrate the presence of well-defined backbone structure within the unfolded states of proteins and peptides. This now puts into question prevailing views of unfolded proteins and alternatives must now be sought.",

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AB - Random coil has a long history of interpreting experimental results on unfolded proteins, in particular those from hydrodynamic and SAXS measurements of the radius of gyration (Rg). However, the model is inconsistent with older observations from Krimm's group as well as a wealth of spectroscopic techniques that demonstrate the presence of well-defined backbone structure within the unfolded states of proteins and peptides. This now puts into question prevailing views of unfolded proteins and alternatives must now be sought.

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Conformation of the backbone in unfolded proteins

Abstract

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