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Volumn 19, Issue 2, 2001, Pages 153-165

Chemical shifts in denatured proteins: Resonance assignments for denatured ubiquitin and comparisons with other denatured proteins

(4) Peti, W a Smith, L J b Redfield, C b Schwalbe, H c

a GOETHE UNIVERSITY (Germany)

b UNIVERSITY OF OXFORD (United Kingdom)

c MASSACHUSETTS INSTITUTE OF TECHNOLOGY (United States)

Author keywords

lactalbumin; Chemical shifts; Denatured proteins; Lysozyme; Random coil; Resonance assignment; Triple resonance NMR; Ubiquitin

Indexed keywords

ALANINE; ALPHA LACTALBUMIN; DISULFIDE; LYSOZYME; UBIQUITIN; UREA;

ANALYSIS; ARTICLE; CONTROLLED STUDY; DATA BASE; MEASUREMENT; PARAMETER; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN METHYLATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

ANIMALS; HUMANS; LACTALBUMIN; MAGNETIC RESONANCE SPECTROSCOPY; MURAMIDASE; NITROGEN ISOTOPES; PROTEIN DENATURATION; UBIQUITINS;

EID: 0035119625 PISSN: 09252738 EISSN: None Source Type: Journal
DOI: 10.1023/A:1008307323283 Document Type: Article

Times cited : (70)

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