Stable intermediates determine proteins' primary unfolding sites in the presence of surfactants

Biopolymers

Volumn 91, Issue 3, 2009, Pages 221-231

  Hansen, Jonas Høeg ^a   Petersen, Steen Vang ^b,c,d   Andersen, Kell Kleiner ^a,b,c   Enghild, Jan J ^b,c   Damhus, Ture ^e   Otzen, Daniel ^a,b,c  

^a AALBORG UNIVERSITY   (Denmark)

^b AARHUS UNIVERSITY   (Denmark)

^c AARHUS UNIVERSITY   (Denmark)

^d NOVOZYMES A S   (Denmark)

^e Institute of Medical Biochemistry   (Denmark)

Author keywords

Alcalase; Flexibility; N terminal sequencing unfolding; Protein substrates; Savinase; Surfactant

Indexed keywords

ALCALASE; FLEXIBILITY; N-TERMINAL SEQUENCING UNFOLDING; PROTEIN SUBSTRATES; SAVINASE; SURFACTANT;

BINDING SITES; DIFFUSERS (OPTICAL); DYES; ORGANIC SOLVENTS; STOICHIOMETRY; SURFACE ACTIVE AGENTS;

PROTEIN FOLDING;

ALPHA LACTALBUMIN; ANIONIC SURFACTANT; CATIONIC SURFACTANT; MYOGLOBIN; SOLVENT; SUBTILISIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; ENZYME SPECIFICITY; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STOICHIOMETRY;

ANIMALS; CATTLE; MODELS, MOLECULAR; PEPTIDE HYDROLASES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; SODIUM DODECYL SULFATE; SUBSTRATE SPECIFICITY; SURFACE-ACTIVE AGENTS; TEMPERATURE;

EID: 65249157372     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21125     Document Type: Article

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