Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus

Proteins: Structure, Function and Genetics

Volumn 62, Issue 1, 2006, Pages 64-79

  Corazza, Alessandra ^a   Rosano, Camillo ^b   Pagano, Katiuscia ^a   Alverdi, Vera ^a   Esposito, Gennaro ^a   Capanni, Cristina ^c   Bemporad, Francesco ^c   Plakoutsi, Georgia ^c   Stefani, Massimo ^c   Chiti, Fabrizio ^c   Zuccotti, Simone ^d   Bolognesi, Martino ^d,e   Viglino, Paolo ^a  

^a UNIVERSITY OF UDINE   (Italy)

^b UNIVERSITY OF GENOA   (Italy)

^c UNIVERSITY OF FLORENCE   (Italy)

^d UNIVERSITY OF GENOA   (Italy)

^e UNIVERSITY OF MILAN   (Italy)

Author keywords

1H NMM spectroscopy; Protein structure; Protein thermostability; Sulfolobus solfataricus acylphosphatase; X ray crystallography

Indexed keywords

ACYLPHOSPHATASE; ARGININE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; ENERGY; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; MELTING POINT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FAMILY; PROTON NUCLEAR MAGNETIC RESONANCE; ROOM TEMPERATURE; STRUCTURE ANALYSIS; SULFOLOBUS SOLFATARICUS; TEMPERATURE DEPENDENCE; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY;

ACID ANHYDRIDE HYDROLASES; ARCHAEAL PROTEINS; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; PROTEIN CONFORMATION; SCATTERING, RADIATION; SULFOLOBUS; THERMODYNAMICS;

ARCHAEA; SULFOLOBUS SOLFATARICUS;

EID: 30344478570     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20703     Document Type: Article

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