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Biochemistry

Volumn 40, Issue 39, 2001, Pages 11923-11931

Thermodynamic stability of the bacteriorhodopsin lattice as measured by lipid dilution

(2) Isenbarger, T A a,b Krebs, M P a,c

a UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH (United States)

b HARVARD MEDICAL SCHOOL (United States)

c ILLINOIS STATE UNIVERSITY (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT LATTICES;

AMINO ACIDS; BACTERIA; CONCENTRATION (PROCESS); CRYSTAL LATTICES; CRYSTAL STRUCTURE; ENTROPY; LIPIDS; PROTEINS; SELF ASSEMBLY; SPECTROSCOPIC ANALYSIS; THERMODYNAMICS;

BIOCHEMISTRY;

ALANINE; AMINO ACID; BACTERIORHODOPSIN; GLYCINE; PHOSPHATIDYLCHOLINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CALCULATION; CIRCULAR DICHROISM; COMPLEX FORMATION; CONCENTRATION RESPONSE; CRYSTAL STRUCTURE; DILUTION; DISSOCIATION; ENTROPY; LIPID BILAYER; MEASUREMENT; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN LIPID INTERACTION; PROTEIN PROTEIN INTERACTION; QUANTITATIVE ASSAY; SEQUENCE ANALYSIS; THERMODYNAMICS; THERMOSTABILITY; TITRIMETRY;

BACTERIORHODOPSINS; CIRCULAR DICHROISM; LIPID BILAYERS; LIPIDS; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; PROTEIN CONFORMATION; THERMODYNAMICS;

BACTERIA (MICROORGANISMS);

EID: 0035797893 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi0106585 Document Type: Article

Times cited : (14)

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