Dynamics and orientation of amphipathic peptides in solution and bound to membranes: A steady-state and time-resolved fluorescence study of staphylococcal δ-toxin and its synthetic analogues

European Biophysics Journal

Volumn 30, Issue 2, 2001, Pages 147-161

  Bull, David A ^a   Connors, Rafe C ^a   Albanil, Aida ^a   Reid, Bruce B ^a   Neumayer, Leigh A ^a   Nelson, Ryan ^a   Stringham, James C ^a   Karwande, Shreekanth V ^a  

^a UNIVERSITY OF UTAH HEALTH SCIENCES CENTER   (United States)

Author keywords

Fluorescence quenching; Mobility; Self association; Time resolved fluorescence anisotropy; Toxin

Indexed keywords

AMPHOPHILE; STAPHYLOCOCCUS ALPHA TOXIN;

ANISOTROPY; ARTICLE; DISSOCIATION; FLUORESCENCE; HYDROPHILICITY; HYDROPHOBICITY; LIPID VESICLE; MATHEMATICAL ANALYSIS; MOLECULAR DYNAMICS; OLIGOMERIZATION; PHOSPHOLIPID VESICLE; PROTEIN INTERACTION; STEADY STATE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL TOXINS; BINDING SITES; CELL MEMBRANE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; KINETICS; LIGHT; LIPID BILAYERS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; PEPTIDES; PHOSPHATIDYLCHOLINES; PHOSPHATIDYLSERINES; SCATTERING, RADIATION; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP; TRYPTOPHAN;

STAPHYLOCOCCUS;

EID: 0034880883     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490000118     Document Type: Article

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