De novo design, synthesis and solution conformational study of two didehydroundecapeptides: Effect of nature and number of amino acids interspersed between Phe residues

Journal of Peptide Science

Volumn 17, Issue 12, 2011, Pages 783-790

  Dutta, Madhvi Gupta ^a   Mathur, Puniti ^b   Chauhan, Virander S ^a  

^a INTERNATIONAL CENTRE FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Italy)

^b AMITY UNIVERSITY   (India)

Author keywords

; helical conformation; branched residues; didehydrophenylalanine ( Phe); 3 10 helical conformation; Circular dichroism; De novo design; Nuclear magnetic resonance; Simulated annealing

Indexed keywords

ALPHA,BETA DIDEHYDROAMINO ACID; ALPHA,BETA DIDEHYDROPHENYLALANINE; ISOLEUCINE; PHENYLALANINE; POLYPEPTIDE; UNCLASSIFIED DRUG; VALINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; SOLID PHASE SYNTHESIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACIDS; CIRCULAR DICHROISM; MAGNETIC RESONANCE SPECTROSCOPY; OLIGOPEPTIDES; PHENYLALANINE; PROTEIN STABILITY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 81155137929     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1402     Document Type: Article

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