Helix mutations stabilize a late productive intermediate on the folding pathway of ubiquitin

Biochemistry

Volumn 47, Issue 31, 2008, Pages 8225-8236

  Rea, Anita M ^a   Simpson, Emma R ^a,b   Crespo, Maria D ^a,c   Searle, Mark S ^a  

^a UNIVERSITY OF NOTTINGHAM   (United Kingdom)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^c ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

EPITAXIAL GROWTH;

BIPHASIC; COLLISION MODELS; FOLDING PATHWAY; HELICAL PROPENSITY; HELIX STABILITY; RATE-LIMITING; REFOLDING; UBIQUITIN; WILD-TYPE;

PROTEINS;

UBIQUITIN;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; COLLISIONALLY ACTIVATED DISSOCIATION; DNA HELIX; MOLECULAR MODEL; MUTATIONAL ANALYSIS; PHASE TRANSITION; PREDICTION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; UBIQUITINATION; WILD TYPE;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE; THERMODYNAMICS; UBIQUITIN;

EID: 48649105144     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800722d     Document Type: Article

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