Diproline templates as folding nuclei in designed peptides. Conformational analysis of synthetic peptide helices containing amino terminal Pro-Pro segments

Journal of the American Chemical Society

Volumn 128, Issue 24, 2006, Pages 7916-7928

  Rai, Rajkishor ^a   Aravinda, Subrayashastry ^a   Kanagarajadurai, Karuppiah ^a   Raghothama, Srinivasarao ^a   Shamala, Narayanaswamy ^a   Balaram, Padmanabhan ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; CRYSTALS; HYDROGEN BONDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; X RAY DIFFRACTION;

DIPROLINE; ENERGY MINIMIZATION; RAPID DYNAMIC EXCHANGE; TRANS CONFORMERS;

POLYPEPTIDES;

DIMETHYL SULFOXIDE; DIPROLINE; LEUCINE; METHANOL; PHENYLALANINE; PROLINE; SOLVENT; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CIS TRANS ISOMERISM; CRYSTAL STRUCTURE; ENERGY CONSERVATION; HYDROGEN BOND; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; X RAY DIFFRACTION;

BASE SEQUENCE; CHLOROFORM; CRYSTALLOGRAPHY, X-RAY; DIPEPTIDES; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLVENTS;

EID: 33745360908     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja060674v     Document Type: Article

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