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Volumn 34, Issue 3, 2006, Pages 129-135
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Assessment of the effects of increased relaxation dispersion data on the extraction of 3-site exchange parameters characterizing the unfolding of an SH3 domain
a a a |
Author keywords
Chemical exchange; CPMG NMR relaxation dispersion; Monte Carlo simulation; Protein folding; SH3 domain
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Indexed keywords
PROTEIN SH3;
ANALYTICAL ERROR;
ARTICLE;
BIOINFORMATICS;
CONTROLLED STUDY;
DATA ANALYSIS;
MONTE CARLO METHOD;
NITROGEN NUCLEAR MAGNETIC RESONANCE;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PROTON NUCLEAR MAGNETIC RESONANCE;
TEMPERATURE DEPENDENCE;
DEUTERIUM EXCHANGE MEASUREMENT;
MONTE CARLO METHOD;
MUTATION;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
PROTEIN FOLDING;
PROTO-ONCOGENE PROTEINS C-FYN;
SRC HOMOLOGY DOMAINS;
TEMPERATURE;
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EID: 33645793984
PISSN: 09252738
EISSN: 15735001
Source Type: Journal
DOI: 10.1007/s10858-006-0001-2 Document Type: Article |
Times cited : (31)
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References (13)
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