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Volumn 14, Issue 2, 2009, Pages 209-217
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Reversible two-step unfolding of heme-human serum albumin: A 1H-NMR relaxometric and circular dichroism study
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Author keywords
1H NMR relaxometry; Circular dichroism; Folding intermediate state; Guanidinium chloride; Heme human serum albumin
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Indexed keywords
GUANIDINE;
HEME;
HUMAN SERUM ALBUMIN;
MYRISTIC ACID;
SATURATED FATTY ACID;
ABSORPTION SPECTROSCOPY;
ARTICLE;
BINDING SITE;
CIRCULAR DICHROISM;
DENATURATION;
HUMAN;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
PROTON NUCLEAR MAGNETIC RESONANCE;
RELAXATION TIME;
SIGNAL TRANSDUCTION;
BINDING SITES;
CIRCULAR DICHROISM;
GUANIDINE;
HEME;
HUMANS;
MAGNETIC RESONANCE SPECTROSCOPY;
MODELS, MOLECULAR;
MYRISTIC ACID;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTONS;
SERUM ALBUMIN;
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EID: 58849167237
PISSN: 09498257
EISSN: None
Source Type: Journal
DOI: 10.1007/s00775-008-0439-7 Document Type: Article |
Times cited : (19)
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References (53)
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