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Journal of Biomolecular NMR

Volumn 19, Issue 1, 2001, Pages 3-18

15N NMR relaxation as a probe for helical intrinsic propensity: The case of the unfolded D2 domain of annexin I

(6) Ochsenbein, F a Guerois, R a Neumann, J M a Sanson, A a Guittet, E a van Heijenoort, C a

a CNRS (France)

Author keywords

15N NMR relaxation; Annexin; Dynamics; Protein folding; Unfolded state

Indexed keywords

DIAGNOSTIC AGENT; LIPOCORTIN 1; NITROGEN; PEPTIDE FRAGMENT; NITROGEN 15;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; MAGNETISM; METHODOLOGY; NONLINEAR SYSTEM; NUCLEAR MAGNETIC RESONANCE; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; CALCULATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; MAGNETIC FIELD; MODEL; MOTION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PARAMETER; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; SPECTROMETRY;

ANNEXIN A1; MAGNETICS; MODELS, MOLECULAR; NITROGEN ISOTOPES; NONLINEAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 0034746293 PISSN: 09252738 EISSN: None Source Type: Journal
DOI: 10.1023/A:1008390606077 Document Type: Article

Times cited : (22)

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