The Denatured State of N-PGK Is Compact and Predominantly Disordered

Journal of Molecular Biology

Volumn 385, Issue 1, 2009, Pages 266-277

  Cliff, Matthew J ^a   Craven, C Jeremy ^a   Marston, James P ^a   Hounslow, Andrea M ^a   Clarke, Anthony R ^b   Waltho, Jonathan P ^a,c  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

^b UNIVERSITY OF BRISTOL   (United Kingdom)

^c UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

folding intermediates; NMR; paramagnetic relaxation enhancement; phosphoglycerate kinase; protein folding

Indexed keywords

AMIDE; CYSTEINE; GUANIDINE; MESYLIC ACID DERIVATIVE; NITROXIDE; PHOSPHOGLYCERATE KINASE; UNCLASSIFIED DRUG; [(1 OXYL 2,2,5,5 TETRAMETHYL 3 PYRROLINE 3 METHYL)METHANESULFONATE];

ARTICLE; CONTROLLED STUDY; DENATURATION; ELECTRON; ENZYME STRUCTURE; EQUILIBRIUM CONSTANT; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; SPIN LABELING;

EID: 57749209980     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.10.004     Document Type: Article

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