Journal article
Conformational propensities and residual structures in unfolded peptides and proteins
Molecular bioSystems, v 8(1)
Jan 2012
PMID: 21879108
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Ample evidence gathered over the last ten years indicates that unfolded and naturally disordered proteins and peptides can show local order in that short segments can adopt turn or polyproline II-like conformations. These findings show that unfolded states cannot be described by the so-called random coil model which assumes that individual amino acid residues sample the entire sterically accessible parts of the Ramachandran with very similar probabilities. This article reviews the experimental evidence for the notion that amino acid residues have different propensities for polyproline II, β-strand, helical and turn conformations in water. These propensities are changed by interactions with nearest neighbours. We show that for a substantial number of residues the conformational propensities in the unfolded state correlate with values for helix propagation and the Chou-Fasman propensities for β-strands. Based on the presented results we hypothesize that the conformational distributions of a representative set of short peptides could be used for predicting structural distributions of disordered peptides and proteins in the future.
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Details
- Title
- Conformational propensities and residual structures in unfolded peptides and proteins
- Creators
- Reinhard Schweitzer-Stenner - Department of Chemistry, Drexel University, Philadelphia, PA 19104, USA. rschweitzer-stenner@drexel.edu
- Publication Details
- Molecular bioSystems, v 8(1)
- Publisher
- Royal Society of Chemistry; England
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:000297561600013
- Scopus ID
- 2-s2.0-82655179918
- Other Identifier
- 991014877878204721
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- Web of Science research areas
- Biochemistry & Molecular Biology