High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins

Methods

Volumn 34, Issue 1, 2004, Pages 133-143

  Kamatari, Yuji O ^a   Kitahara, Ryo ^a   Yamada, Hiroyuki ^b   Yokoyama, Shigeyuki ^a,c,d   Akasaka, Kazuyuki ^a,e  

^a RIKEN HARIMA INSTITUTE   (Japan)

^b KOBE UNIVERSITY   (Japan)

^c RIKEN YOKOHAMA INSTITUTE   (Japan)

^d UNIVERSITY OF TOKYO   (Japan)

^e KINKI UNIVERSITY   (Japan)

Author keywords

Aggregation; Cold denaturation; Helical denatured state; High pressure NMR; Intermediate states; Molten globule; Non native states; Pressure denaturation; Protein folding; Random coiled peptide

Indexed keywords

ARTICLE; DISSOCIATION; EQUILIBRIUM CONSTANT; KINETICS; MOLECULAR MECHANICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; PRESSURE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS;

ANIMALS; APOPROTEINS; LACTOGLOBULINS; MYOGLOBIN; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PRESSURE; PRIONS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; UBIQUITIN;

EID: 3342936435     PISSN: 10462023     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ymeth.2004.03.010     Document Type: Article

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