Acid destabilization of the solution conformation of Bcl-XL does not drive its pH-dependent insertion into membranes

Protein Science

Volumn 15, Issue 2, 2006, Pages 248-257

  Thuduppathy, Guruvasuthevan R ^a   Hill, R Blake ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

Author keywords

Bcl 2 family; Bcl xL; Diphtheria toxin; pH dependence; Pore forming toxins; Protein folding; Solution to membrane conformational change

Indexed keywords

DIPHTHERIA TOXIN; PROTEIN BCL XL; PROTEINASE;

ACIDIFICATION; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENERGY; LIPID VESICLE; MEMBRANE STABILIZATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STABILITY; STATISTICAL SIGNIFICANCE; ULTRAVIOLET RADIATION;

ACIDS; BCL-X PROTEIN; CELL MEMBRANE; CIRCULAR DICHROISM; HUMANS; HYDROGEN-ION CONCENTRATION; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DENATURATION; SOLUTIONS; THERMODYNAMICS;

EID: 31344431883     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051807706     Document Type: Article

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