Number of the records: 1
Insights into Unfolded Proteins from the Intrinsic phi/psi Propensities of the AAXAA Host-Guest Series
- 1.
SYSNO ASEP 0458534 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Insights into Unfolded Proteins from the Intrinsic phi/psi Propensities of the AAXAA Host-Guest Series Author(s) Towse, C. L. (US)
Vymětal, Jiří (UOCHB-X) RID, ORCID
Vondrášek, Jiří (UOCHB-X) RID, ORCID
Daggett, V. (US)Source Title Biophysical Journal. - : Cell Press - ISSN 0006-3495
Roč. 110, č. 2 (2016), s. 348-361Number of pages 14 s. Language eng - English Country US - United States Keywords polyproline-II helix ; beta-sheet protein ; random-coil behavior Subject RIV BO - Biophysics R&D Projects LH11020 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Institutional support UOCHB-X - RVO:61388963 UT WOS 000368354700009 EID SCOPUS 84955447535 DOI 10.1016/j.bpj.2015.12.008 Annotation Various host-guest peptide series are used by experimentalists as reference conformational states. One such use is as a baseline for random-coil NMR chemical shifts. Comparison to this random-coil baseline, through secondary chemical shifts, is used to infer protein secondary structure. The use of these random-coil data sets rests on the perception that the reference chemical shifts arise from states where there is little or no conformational bias. However, there is growing evidence that the conformational composition of natively and nonnatively unfolded proteins fail to approach anything that can be construed as random coil. Here, we use molecular dynamics simulations of an alanine-based host-guest peptide series (AAXAA) as a model of unfolded and denatured states to examine the intrinsic propensities of the amino acids. We produced ensembles that are in good agreement with the experimental NMR chemical shifts and confirm that the sampling of the 20 natural amino acids in this peptide series is be far from random. Preferences toward certain regions of conformational space were both present and dependent upon the environment when compared under conditions typically used to denature proteins, i.e., thermal and chemical denaturation. Moreover, the simulations allowed us to examine the conformational makeup of the underlying ensembles giving rise to the ensemble-averaged chemical shifts. We present these data as an intrinsic backbone propensity library that forms part of our Structural Library of Intrinsic Residue Propensities to inform model building, to aid in interpretation of experiment, and for structure prediction of natively and nonnatively unfolded states. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Year of Publishing 2017
Number of the records: 1