Probing residue-specific interactions in the stabilization of proteins using high-resolution NMR: a study of disulfide bond compensation

Journal of Pharmaceutical Sciences

Volumn 99, Issue 6, 2010, Pages 2643-2654

  Skinner, Andria L ^a   Laurence, Jennifer S ^a  

^a UNIVERSITY OF KANSAS   (United States)

Author keywords

Circular dichroism; Light scattering; Nmr spectroscopy; Oxidation; Physical stability; PRL 1; Protein aggregation; Protein structure

Indexed keywords

CYSTEINE; MUTANT PROTEIN;

ARTICLE; BETA SHEET; CHEMICAL BINDING; CHEMICAL MODEL; CIRCULAR DICHROISM; CONTROLLED STUDY; DISULFIDE BOND; HYDROGEN BOND; MOLECULAR DYNAMICS; MOLECULAR PROBE; NITROGEN NUCLEAR MAGNETIC RESONANCE; PROTEIN AGGREGATION; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

EID: 77951518291     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.22055     Document Type: Article

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