Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins

Methods

Volumn 34, Issue 1, 2004, Pages 121-132

  Redfield, Christina ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Lactalbumin; Apomyoglobin; Chemical shift; HSQC; Hydrogen deuterium exchange; Molten globule; Partially folded proteins; Protein denaturation; Protein folding; Resonance assignment

Indexed keywords

ALPHA LACTALBUMIN; APOMYOGLOBIN; CARBON 13; CARBON MONOXIDE; DEUTERIUM; HYDROGEN; NITROGEN 15;

ARTICLE; CHEMICAL ANALYSIS; CONCENTRATION (PARAMETERS); DENATURATION; ION EXCHANGE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; QUALITATIVE ANALYSIS; RELAXATION TRAINING;

ANIMALS; APOPROTEINS; CATTLE; DEUTERIUM; HUMANS; HYDROGEN; HYDROGEN-ION CONCENTRATION; LACTALBUMIN; MAGNETIC RESONANCE SPECTROSCOPY; MYOGLOBIN; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 3242878900     PISSN: 10462023     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ymeth.2004.03.009     Document Type: Article

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