Conformation of the backbone in unfolded proteins

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

Research output: Contribution to journalReview article

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.

Original languageEnglish (US)
Pages (from-to)1877-1897
Number of pages21
JournalChemical reviews
Volume106
Issue number5
DOIs
StatePublished - May 2006

ASJC Scopus subject areas

  • Chemistry(all)

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    Shi, Z., Chen, K., Liu, Z., & Kallenbach, N. R. (2006). Conformation of the backbone in unfolded proteins. Chemical reviews, 106(5), 1877-1897. https://doi.org/10.1021/cr040433a