NMR studies of the fifth transmembrane segment of sarcoplasmic reticulum Ca2+-ATPase reveals a hinge close to the Ca2+-ligating residues

FEBS Letters

Volumn 544, Issue 1-3, 2003, Pages 50-56

  Nielsen, Gerd ^a   Malmendal, Anders ^a   Meissner, Axel ^b,c   Møller, Jesper V ^a   Nielsen, Niels Chr ^a  

^a AARHUS UNIVERSITY   (Denmark)

^b CARLSBERG LABORATORY   (Denmark)

^c NOVARTIS PHARMA AG   (Switzerland)

Author keywords

Ca2+ ATPase; Fifth transmembrane segment M5; Membrane protein; Micelle; Nuclear magnetic resonance; Sarcoplasmic reticulum; Sodium dodecyl sulfate

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CALCIUM ION; DODECYL SULFATE SODIUM;

ALPHA HELIX; ARTICLE; CALCIUM BINDING; CRYSTAL STRUCTURE; ENDOPLASMIC RETICULUM; LIGATION; MEMBRANE POTENTIAL; MICELLE; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; SARCOPLASMIC RETICULUM; X RAY ANALYSIS; X RAY DIFFRACTION;

EID: 0038356718     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(03)00448-4     Document Type: Article

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