Role of Cysteine Residues in Structural Stability and Function of a Transmembrane Helix Bundle

Journal of Biological Chemistry

Volumn 276, Issue 42, 2001, Pages 38814-38819

  Karim, Christine B ^a   Paterlini, M Germana ^a   Reddy, Laxma G ^a   Hunter, Gregory W ^a   Barany, George ^a   Thomas, David D ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROPHORESIS; ENZYMES; OLIGOMERS; ORGANIC ACIDS;

MOLECULAR MODELING;

BIOCHEMISTRY;

2 AMINOBUTYRIC ACID; 9 FLUORENYLMETHYL CHLOROFORMATE; ADENOSINE TRIPHOSPHATASE (CALCIUM); ALANINE; CYSTEINE; MEMBRANE PROTEIN; METHIONINE; OLIGOMER; PHOSPHOLAMBAN; THIOL DERIVATIVE; AMINO ACID; AMINOBUTYRIC ACID DERIVATIVE; BUTYRINE; CALCIUM BINDING PROTEIN; DETERGENT; FLUORENE DERIVATIVE; LYSOPHOSPHOLIPASE; N(ALPHA) FLUORENYLMETHYLOXYCARBONYLAMINO ACIDS; N(ALPHA)-FLUORENYLMETHYLOXYCARBONYLAMINO ACIDS;

ACETYLATION; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; ENERGY; MOLECULAR MODEL; PEPTIDE SYNTHESIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STABILITY; PROTEIN STRUCTURE; STEREOSPECIFICITY; WILD TYPE; AMINO ACID SEQUENCE; ANIMAL; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; FAST MUSCLE FIBER; KINETICS; MASS SPECTROMETRY; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; RABBIT; SARCOPLASMIC RETICULUM; SKELETAL MUSCLE; TEMPERATURE;

ALANINE; AMINO ACID SEQUENCE; AMINO ACIDS; AMINOBUTYRIC ACIDS; ANIMALS; CALCIUM-BINDING PROTEINS; CALCIUM-TRANSPORTING ATPASES; CELL MEMBRANE; CYSTEINE; DETERGENTS; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FLUORENES; KINETICS; LYSOPHOSPHOLIPASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUSCLE FIBERS, FAST-TWITCH; MUSCLE, SKELETAL; PEPTIDE BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RABBITS; SARCOPLASMIC RETICULUM; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TEMPERATURE;

EID: 0035914315     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M104006200     Document Type: Article

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