The conformation of ATP within the Na,K-ATPase nucleotide site: A statistically constrained analysis of REDOR solid-state NMR data

Angewandte Chemie - International Edition

Volumn 50, Issue 31, 2011, Pages 7041-7044

  Middleton, David A ^a   Hughes, Eleri ^a   Esmann, Mikael ^b  

^a UNIVERSITY OF LIVERPOOL   (United Kingdom)

^b AARHUS UNIVERSITY   (Denmark)

Author keywords

adenosine triphosphate; conformation analysis; NMR spectroscopy; nucleotide ligands; torsional angles

Indexed keywords

CONFORMATION ANALYSIS; CONFORMATIONAL PREFERENCES; NATIVE MEMBRANES; SOLID STATE NMR; TORSIONAL ANGLE;

ADENOSINETRIPHOSPHATE; LIGANDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHATES; SODIUM; SOLID STATE PHYSICS; STRUCTURAL ANALYSIS;

NUCLEOTIDES;

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE;

ANIMAL; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; METABOLISM; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE; SWINE;

ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING SITES; MODELS, MOLECULAR; MOLECULAR CONFORMATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; SODIUM-POTASSIUM-EXCHANGING ATPASE; SWINE;

EID: 79960642324     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201100736     Document Type: Article

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