Using hydrogen-bonding interactions to control the peptide secondary structures and miscibility behavior of poly(l -glutamate)s with phenolic resin

Macromolecules

Volumn 44, Issue 18, 2011, Pages 7315-7326

  Kuo, Shiao Wei ^a   Chen, Chi Jen ^a  

^a NATIONAL SUN YAT SEN UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION MODELS; BINARY BLENDS; BLEND SYSTEM; FOURIER TRANSFORM INFRARED; FTIR; HELICAL CONFORMATION; HYDROGEN BOND ACCEPTORS; HYDROGEN BONDING INTERACTIONS; INTERMOLECULAR HYDROGEN BONDING; L-GLUTAMATE; LOW MOLECULAR WEIGHT; MISCIBILITY BEHAVIOR; PEPTIDE SECONDARY STRUCTURES; PHENOLIC CONTENT; POLY(GLUTAMATE); PROTON SPIN LATTICE RELAXATION; ROTATING FRAME; SECONDARY STRUCTURES; SIDE-CHAINS; SINGLE GLASS TRANSITION; SOLID STATE NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLID-STATE NMR SPECTROSCOPY; VARIABLE-TEMPERATURE INFRARED SPECTROSCOPY;

AMINO ACIDS; CONFORMATIONS; DIFFERENTIAL SCANNING CALORIMETRY; FOURIER TRANSFORMS; GLASS TRANSITION; HYDROGEN BONDS; INFRARED SPECTROSCOPY; LIVING POLYMERIZATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES; PHENOLIC RESINS; POLYPEPTIDES; RESINS; RING OPENING POLYMERIZATION; SPIN GLASS;

PHENOLS;

EID: 80053005610     PISSN: 00249297     EISSN: None     Source Type: Journal    
DOI: 10.1021/ma200721e     Document Type: Article

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