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Literature DB >> 1489908

Residue solvent accessibilities in the unfolded polypeptide chain.

Abstract

The difference of solvent accessibilities in the native and unfolded states of the protein is used as a measure of the hydrophobic contribution to the free energy of folding. We present a new approximation of amino acids solvent accessibilities in the unfolded state based on the 1-ns molecular dynamics simulation of Ala-X-Ala tripeptides at a temperature of 368 K. The standard accessibility values averaged from the molecular dynamics study are significantly lower from those previously obtained by considering only selected conformations of Ala-X-Ala tripeptides.

Entities: Chemical

Mesh：

Substances：
Oligopeptides
Solvents

Year: 1992 PMID： 1489908 PMCID： PMC1262262 DOI： 10.1016/S0006-3495(92)81746-0

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

16 in total

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7 in total

1. Sequence-specific solvent accessibilities of protein residues in unfolded protein ensembles.

Authors: Pau Bernadó; Martin Blackledge; Javier Sancho
Journal: Biophys J Date: 2006-09-29 Impact factor: 4.033

2. A double-deletion method to quantifying incremental binding energies in proteins from experiment: example of a destabilizing hydrogen bonding pair.

Authors: Luis A Campos; Santiago Cuesta-López; Jon López-Llano; Fernando Falo; Javier Sancho
Journal: Biophys J Date: 2004-11-19 Impact factor: 4.033

3. Stacking and energetic contribution of aromatic islands at the binding interface of antibody proteins.

Authors: Di Wu; Jing Sun; Tianlei Xu; Shuning Wang; Guoqing Li; Yixue Li; Zhiwei Cao
Journal: Immunome Res Date: 2010-09-27

4. Semirational Directed Evolution of Loop Regions in Aspergillus japonicus β-Fructofuranosidase for Improved Fructooligosaccharide Production.

Authors: K M Trollope; J F Görgens; H Volschenk
Journal: Appl Environ Microbiol Date: 2015-08-07 Impact factor: 4.792