Dynamics fingerprint and inherent asymmetric flexibility of a cold-adapted homodimeric enzyme. A case study of the Vibrio alkaline phosphatase

Biochimica et Biophysica Acta - General Subjects

Volumn 1830, Issue 4, 2013, Pages 2970-2980

  Papaleo, Elena ^a   Renzetti, Giulia ^a   Invernizzi, Gaetano ^a   Ásgeirsson, Bjarni ^b  

^a UNIVERSITY OF MILANO BICOCCA   (Italy)

^b UNIVERSITY OF ICELAND   (Iceland)

Author keywords

Alkaline phosphatase; Asymmetric flexibility; Cold adapted; Crown domain; Molecular dynamics; Psychrophilic

Indexed keywords

ALKALINE PHOSPHATASE; HOMODIMER; MONOMER;

ARTICLE; BACTERIAL STRAIN; CASE STUDY; CORRELATION ANALYSIS; ENZYME ACTIVITY; ENZYME ANALYSIS; LOW TEMPERATURE; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; VIBRIO;

ALKALINE PHOSPHATASE; COLD TEMPERATURE; MOLECULAR DYNAMICS SIMULATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; VIBRIO;

VIBRIO;

EID: 84873734964     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2012.12.011     Document Type: Article

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