Files and links (1)
Published, Version of Record (VoR)CC BY V4.0, Open
Journal article
Local order in the unfolded state: conformational biases and nearest neighbor interactions
Biomolecules (Basel, Switzerland), v 4(3), pp 725-773
24 Jul 2014
PMID: 25062017
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The discovery of Intrinsically Disordered Proteins, which contain significant levels of disorder yet perform complex biologically functions, as well as unwanted aggregation, has motivated numerous experimental and theoretical studies aimed at describing residue-level conformational ensembles. Multiple lines of evidence gathered over the last 15 years strongly suggest that amino acids residues display unique and restricted conformational preferences in the unfolded state of peptides and proteins, contrary to one of the basic assumptions of the canonical random coil model. To fully understand residue level order/disorder, however, one has to gain a quantitative, experimentally based picture of conformational distributions and to determine the physical basis underlying residue-level conformational biases. Here, we review the experimental, computational and bioinformatic evidence for conformational preferences of amino acid residues in (mostly short) peptides that can be utilized as suitable model systems for unfolded states of peptides and proteins. In this context particular attention is paid to the alleged high polyproline II preference of alanine. We discuss how these conformational propensities may be modulated by peptide solvent interactions and so called nearest-neighbor interactions. The relevance of conformational propensities for the protein folding problem and the understanding of IDPs is briefly discussed.
Metrics
Details
- Title
- Local order in the unfolded state: conformational biases and nearest neighbor interactions
- Creators
- Siobhan Toal - Drexel UniversityReinhard Schweitzer-Stenner - Drexel University
- Publication Details
- Biomolecules (Basel, Switzerland), v 4(3), pp 725-773
- Publisher
- MDPI
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]; Chemistry
- Web of Science ID
- WOS:000215156000007
- Scopus ID
- 2-s2.0-84924366750
- Other Identifier
- 991019167931804721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology