Membrane protein stability depends on the concentration of compatible solutes - A single molecule force spectroscopic study

Biological Chemistry

Volumn 394, Issue 11, 2013, Pages 1465-1474

  Roychoudhury, Arpita ^a   Bieker, Adeline ^a   Häussinger, Dieter ^a   Oesterhelt, Filipp ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

Author keywords

Atomic force microscopy; Compatible solutes; Membrane proteins; Osmolytes; Protein unfolding; Single molecule force spectroscopy

Indexed keywords

BACTERIORHODOPSIN; BETAINE; ECTOINE; POLYPEPTIDE; TAURINE;

ARTICLE; ATOMIC FORCE MICROSCOPY; FORCE; MEMBRANE; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN UNFOLDING; SINGLE MOLECULE FORCE SPECTROSCOPY; SOLUTE; STRESS;

AMINO ACIDS, DIAMINO; BACTERIORHODOPSINS; BETAINE; HALOBACTERIUM SALINARUM; MEMBRANE PROTEINS; MICROSCOPY, ATOMIC FORCE; OSMOTIC PRESSURE; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING; SOLUTIONS; SPECTRUM ANALYSIS; TAURINE; WATER;

EID: 84888083001     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2013-0173     Document Type: Article

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