Local conformation of serine residues in a silk model peptide, (Ala-Gly-Ser-Gly-Ala-Gly)5, studied with solid-state NMR:REDOR

Polymer Journal

Volumn 42, Issue 4, 2010, Pages 354-356

  Suzuki, Yu ^a   Asakura, Tetsuo ^a  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC DISTANCES; MODEL PEPTIDES; ROTATIONAL ECHO DOUBLE RESONANCE; SERINE RESIDUES; SILK FIBROIN; SOLID STATE NMR;

AMINO ACIDS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHATASES; SILK; SOLID STATE PHYSICS;

PEPTIDES;

EID: 77951051647     PISSN: 00323896     EISSN: 13490540     Source Type: Journal    
DOI: 10.1038/pj.2010.2     Document Type: Article

References (11)

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