Aromatic residues engineered into the β-turn nucleation site of ubiquitin lead to a complex folding landscape, non-native side-chain interactions, and kinetic traps

Biochemistry

Volumn 47, Issue 48, 2008, Pages 12910-12922

  Rea, Anita M ^a   Simpson, Emma R ^a,b   Meldrum, Jill K ^a   Williams, Huw E L ^a   Searle, Mark S ^a  

^a UNIVERSITY OF NOTTINGHAM   (United Kingdom)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; AROMATIC COMPOUNDS; FLOW INTERACTIONS; FORMING; NUCLEATION; PORT TERMINALS; POWDERS; PROTEINS;

A STABLES; AMYLOID FORMATIONS; AROMATIC RESIDUES; AROMATIC SUBSTITUTIONS; CHAIN INTERACTIONS; EVOLUTIONARY PRESSURES; FOLDED STATES; FOLDING KINETICS; FOLDING PATHWAYS; HYDROPHOBIC CONTACTS; KINETIC PHASE; KINETIC TRAPS; NATIVE STATES; NUCLEATION SITES; REFOLDING; TRANSITION STATES; UBIQUITIN;

PROTEIN FOLDING;

UBIQUITIN;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CONFORMATIONAL TRANSITION; KINETICS; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STABILITY;

AMINO ACID SEQUENCE; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; FUNGAL PROTEINS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POINT MUTATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; UBIQUITIN;

EID: 57049128788     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801330r     Document Type: Article

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