The preferred conformation of the tripeptide Ala-Phe-Ala in water is an inverse γ-turn: Implications for protein folding and drug design

Biochemistry

Volumn 44, Issue 43, 2005, Pages 14170-14178

  Motta, Andrea ^a   Reches, Meital ^b   Pappalardo, Lucia ^a   Andreotti, Giuseppina ^a   Gazit, Ehud ^b  

^a CNR   (Italy)

^b TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; FOURIER TRANSFORM INFRARED SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE; NUCLEATION; PROTEINS; WATER;

CIRCULAR DICHROISM (CD); DRUG DESIGN; PEPTIDOMIMETIC DRUGS; TRIPEPTIDES;

DRUG PRODUCTS;

ALANYLPHENYLALANYLALANINE; PEPTIDE DERIVATIVE; SOLVENT; TRIPEPTIDE; UNCLASSIFIED DRUG; WATER;

AMINO ACID SEQUENCE; AQUEOUS SOLUTION; ARTICLE; BETA SHEET; CALCULATION; CARBON NUCLEAR MAGNETIC RESONANCE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DRUG DESIGN; HYDROGEN BOND; INFRARED SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STEREOSPECIFICITY; STRUCTURE ANALYSIS; TECHNIQUE;

ALANINE; CIRCULAR DICHROISM; DRUG DESIGN; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR CONFORMATION; MOLECULAR MIMICRY; OLIGOPEPTIDES; PROTEIN FOLDING; SOLVENTS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; WATER;

EID: 27444446525     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050658v     Document Type: Article

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