Membrane depth-dependent energetic contribution of the tryptophan side chain to the stability of integral membrane proteins

Biochemistry

Volumn 52, Issue 25, 2013, Pages 4413-4421

  Hong, Heedeok ^a   Rinehart, Dennis ^b   Tamm, Lukas K ^b  

^a MICHIGAN STATE UNIVERSITY   (United States)

^b UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; HYDROPHOBIC SURFACES; HYDROPHOBICITY SCALE; INTEGRAL MEMBRANE PROTEINS; MODERATE CONCENTRATION; OUTER MEMBRANE PROTEIN A; TRYPTOPHAN RESIDUES; TRYPTOPHAN SIDE CHAIN;

AMINO ACIDS; HYDROPHOBICITY; LIPID BILAYERS; STABILITY; SURFACE CHEMISTRY; UREA;

PROTEINS;

OUTER MEMBRANE PROTEIN A; TRYPTOPHAN; UREA; WATER;

ARTICLE; BETA SHEET; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENERGY TRANSFER; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; LIPID BILAYER; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN UNFOLDING; QUANTITATIVE ANALYSIS; THERMODYNAMICS; THERMOSTABILITY;

BACTERIAL OUTER MEMBRANE PROTEINS; ENERGY METABOLISM; LIPID BILAYERS; MEMBRANE PROTEINS; MUTAGENESIS, SITE-DIRECTED; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING; THERMODYNAMICS; TRYPTOPHAN;

EID: 84879528225     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400344b     Document Type: Article

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