Role of different β-turns in β-hairpin conformation and stability studied by optical spectroscopy

Proteins: Structure, Function and Bioinformatics

Volumn 80, Issue 1, 2012, Pages 44-60

  Wu, Ling ^a   Mcelheny, Dan ^a   Setnicka, Vladimír ^a,b   Hilario, Jovencio ^a,c   Keiderling, Timothy A ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^b INSTITUTE OF CHEMICAL TECHNOLOGY   (Czech Republic)

^c BIO RAD LABORATORIES   (United States)

Author keywords

turn; DPro Gly; Hairpin peptide; NMR peptide structure; Thermodynamic folding analysis; Tryptophan

Indexed keywords

PROTEIN; PROTEIN BETA HAIRPIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE SPECTROSCOPY; HYDROGEN BOND; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; INFRARED SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN UNFOLDING;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS; TRANSITION TEMPERATURE;

EID: 83555176386     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23140     Document Type: Article

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