Solid-state nuclear magnetic resonance (NMR) spectroscopy reveals distinctive protein dynamics in closely related spider silks

Canadian Journal of Chemistry

Volumn 89, Issue 9, 2011, Pages 1047-1054

  Cloutier, Isabelle ^a   Leclerc, Jérémie ^a   Lefèvre, Thierry ^a   Auger, Michèle ^a  

^a UNIVERSITÉ LAVAL   (Canada)

Author keywords

Dynamics; Reeling speed; Silk proteins; Solid state nuclear magnetic resonance (NMR); Structure

Indexed keywords

AMORPHOUS REGIONS; CHAIN PACKING; COCOON SILK; INTERMOLECULAR INTERACTIONS; MAJOR AMPULLATE; MOLECULAR REARRANGEMENT; NMR SPECTRUM; PROTEIN DYNAMICS; RELAXATION DYNAMICS; RESIDUE LEVEL; SECONDARY STRUCTURES; SILK PROTEINS; SOLID STATE NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLID-STATE NUCLEAR MAGNETIC RESONANCE; SPIDER SILKS; STRUCTURAL DATA; STRUCTURAL ORGANIZATION;

AMINO ACIDS; DYNAMICS; MECHANICAL PROPERTIES; MOLECULAR ORIENTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; RELAXATION PROCESSES; RESONANCE; SILK; SPINNING (FIBERS);

NUCLEAR MAGNETIC RESONANCE;

AMINO ACIDS; MECHANICAL PROPERTIES; NUCLEAR MAGNETIC RESONANCE; PROTEINS; RELAXATION; SILK; SPINNING; WINDING;

EID: 80052449391     PISSN: 00084042     EISSN: None     Source Type: Journal    
DOI: 10.1139/v11-036     Document Type: Article

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