Modulation of p -cyanophenylalanine fluorescence by amino acid side chains and rational design of fluorescence probes of α-helix formation

Biochemistry

Volumn 49, Issue 29, 2010, Pages 6290-6295

  Taskent Sezgin, Humeyra ^a   Marek, Peter ^a   Thomas, Rosanne ^a   Goldberg, Daniel ^a   Chung, Juah ^a   Carrico, Isaac ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO GROUP; AMYLOID FORMATION; CYANO GROUPS; FLUORESCENCE PROBES; FLUORESCENCE QUANTUM YIELD; FLUORESCENCE QUENCHERS; HELIX FORMATION; HIGH-SENSITIVITY; HYDROGEN BONDINGS; HYDROXIDE IONS; NEUTRAL IMIDAZOLE; PROTEIN STRUCTURES; PROTEIN-MEMBRANE INTERACTIONS; PROTEIN-PEPTIDE INTERACTIONS; PROTONATED; RATIONAL DESIGN; SIDE CHAINS; SIDE-CHAIN; STERN-VOLMER CONSTANTS; SYSTEMATIC STUDY;

AMINO ACIDS; HYDROGEN BONDS; ORGANIC ACIDS; PEPTIDES; PROBES; PROTEIN FOLDING; PROTONATION;

FLUORESCENCE;

4 CYANOPHENYLALANINE; ALANINE DERIVATIVE; AMYLOID; ARGININE; ASPARAGINE; CYSTEINE; HISTIDINE; HYDROXIDE; IMIDAZOLE; LYSINE; METHIONINE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; FLUORESCENCE; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON TRANSPORT; QUANTUM YIELD; SENSITIVITY ANALYSIS;

ALANINE; AMINO ACIDS; FLUORESCENCE; FLUORESCENT DYES; HYDROGEN BONDING; HYDROXIDES; IMIDAZOLES; NITRILES; PEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 77954823020     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100932p     Document Type: Article

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