Role of disulfide bonds in conformational stability and folding of 5′-deoxy-5′-methylthioadenosine phosphorylase II from the hyperthermophilic archaeon Sulfolobus solfataricus

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1824, Issue 10, 2012, Pages 1136-1143

  Cacciapuoti, Giovanna ^a,b   Fuccio, Francesca ^a   Petraccone, Luigi ^c   Del Vecchio, Pompea ^c   Porcelli, Marina ^a,b  

^a SECOND UNIVERSITY OF NAPLES   (Italy)

^b NATIONAL INSTITUTE OF BIOSTRUCTURES AND BIOSYSTEMS   (Italy)

^c UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

5 deoxy 5 methylthioadenosine phosphorylase II from Sulfolobus solfataricus; Conformational stability; Disulfide bond; Hyperthermophilic protein; Reversible chemical and thermal unfolding

Indexed keywords

5' DEOXY 5' METHYLTHIOADENOSINE PHOSPHORYLASE II; GUANIDINE; PHOSPHINE DERIVATIVE; PHOSPHORYLASE; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; DENATURATION; DISSOCIATION; DISULFIDE BOND; FLUORESCENCE SPECTROSCOPY; HEATING; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN UNFOLDING; SULFOLOBUS SOLFATARICUS; THERMAL DENATURATION; THERMOSTABILITY;

CIRCULAR DICHROISM; DISULFIDES; ENZYME STABILITY; HOT TEMPERATURE; PROTEIN CONFORMATION; PURINE-NUCLEOSIDE PHOSPHORYLASE; SPECTROMETRY, FLUORESCENCE; SULFOLOBUS SOLFATARICUS;

ARCHAEA; SULFOLOBUS SOLFATARICUS;

EID: 84864120395     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.06.014     Document Type: Article

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