The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs-Reference-Cited by-同舟云学术

The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs

Published:2023 Issue:15 Volume:13 Page:10182-10203
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Kovács Dániel¹²,Bodor Andrea¹^ORCID

Affiliation:

1. ELTE, Eötvös Loránd University, Institute of Chemistry, Analytical and BioNMR Laboratory, Pázmány Péter sétány 1/A, Budapest 1117, Hungary

2. Eötvös Loránd University, Hevesy György PhD School of Chemistry, Pázmány Péter sétány 1/A, Budapest 1117, Hungary

Abstract

In studying secondary structural propensities of proteins by nuclear magnetic resonance (NMR) spectroscopy, secondary chemical shifts (SCSs) are the primary atomic scale observables. But which random coil chemical shift (RCCS) values to choose?

Funder

National Research, Development and Innovation Office

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2023/RA/D3RA00977G

Reference149 articles.

1. Nitrogen-15 chemical shifts of backbone amides in bovine pancreatic trypsin inhibitor and apamin

2. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

3. Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts

4. Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. A computational approach to design a multiepitope vaccine against H5N1 virus;Virology Journal;2024-03-20