Isolated noncatalytic and catalytic subunits of F1-ATPase exhibit similar, albeit not identical, energetic strategies for recognizing adenosine nucleotides

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1837, Issue 1, 2014, Pages 44-50

  Salcedo, Guillermo ^a   Cano Sánchez, Patricia ^a   De Gómez Puyou, Marietta Tuena ^b   Velázquez Campoy, Adrián ^c,d   García Hernández, Enrique ^a  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^b INSTITUTO DE FISIOLOGÍA CELULAR   (Mexico)

^c UNIVERSITY OF ZARAGOZA   (Spain)

^d FUNDACIÓN ARAID   (Spain)

Author keywords

Binding energetics; F1 ATPase; Heterotropic cooperativity; Isolated subunit; Isothermal titration calorimetry; Metal binding

Indexed keywords

ADENOSINE; ADENOSINE DIPHOSPHATE; ADENOSINE DIPHOSPHATE (MAGNESIUM); ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (MAGNESIUM); ADENOSINE TRIPHOSPHATE; APYRASE; F1 ADENOSINE TRIPHOSPHATASE; MAGNESIUM; UNCLASSIFIED DRUG;

ALPHA CHAIN; ARTICLE; BETA CHAIN; BINDING AFFINITY; CELL VOLUME; CONTROLLED STUDY; ENTHALPY; ENZYME ACTIVE SITE; GEOBACILLUS; ISOTHERMAL TITRATION CALORIMETRY; METAL BINDING; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; STOICHIOMETRY; THERMODYNAMICS;

EID: 84884319334     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.08.005     Document Type: Article

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