A fragment of staphylococcal nuclease with an OB-fold structure shows hydrogen-exchange protection factors in the range reported for “molten globules”-Reference-Cited by-同舟云学术

A fragment of staphylococcal nuclease with an OB-fold structure shows hydrogen-exchange protection factors in the range reported for “molten globules”

Published:1996-09 Issue:9 Volume:5 Page:1942-1946
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Sci.

Author:

Alexandrescu Andrei T.,Dames Sonja A.,Wiltscheck Ronald

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference38 articles.

1. NMR structure of a stable “OB-fold” sub-domain isolated from staphylococcal nuclease;Alexandrescu;J Mol Biol,1995

2. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tic Ornithodos moubata;Antuch;FEBS Lett,1994

3. Primary structure effects on peptide group hydrogen exchange;Bai;Proteins Struct Funct Genet,1993

4. Protein folding intermediates studied by native-state hydrogen exchange;Bai;Science,1995

5. Pulsed H/D-exchange studies of folding intermediates;Baldwin;Curr Opin Struct Biol,1993

Cited by 13 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. Protein Conformational Disorder and Enzyme Catalysis;Dynamics in Enzyme Catalysis;2013

2. Impact of the C-terminal Disulfide Bond on the Folding and Stability of Onconase;ChemBioChem;2010-03-26

3. Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra;Protein Science;2008-12-31

4. Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange;Protein Science;2008-12-31

5. β-Hairpins with native-like and non-native hydrogen bonding patterns could form during the refolding of staphylococcal nuclease;Journal of Molecular Graphics and Modelling;2006-09