PH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk - Implications for fiber formation

Angewandte Chemie - International Edition

Volumn 50, Issue 1, 2011, Pages 310-313

  Hagn, Franz ^a   Thamm, Christopher ^b   Scheibel, Thomas ^b   Kessler, Horst ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

biopolymers; circular dichroism; NMR spectroscopy; protein folding; protein structure

Indexed keywords

CIRCULAR DICHROISM; FIBER ASSEMBLIES; FIBER FORMATION; HIGH SALT CONCENTRATION; MONOMER-DIMER EQUILIBRIUM; N-TERMINAL DOMAINS; NEUTRAL PH; NMR SPECTROSCOPY; PH VALUE; PH-DEPENDENT; PROTEIN FIBERS; PROTEIN STRUCTURE; SILK PROTEINS; SPIDER DRAGLINE SILK;

BIOMOLECULES; BIOPOLYMERS; DICHROISM; DIMERS; FIBERS; MONOMERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN FOLDING; SILK;

CIRCULAR DICHROISM SPECTROSCOPY;

FIBROIN; INORGANIC SALT;

ANIMAL; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; DIMERIZATION; DRUG EFFECT; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PROTEIN CONFORMATION; PROTEIN FOLDING; SILK; SPIDER;

ANIMALS; CIRCULAR DICHROISM; DIMERIZATION; FIBROINS; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN FOLDING; SALTS; SILK; SPIDERS;

CIRCULAR DICHROISM; DIMERS; FIBERS; MONOMERS; NUCLEAR MAGNETIC RESONANCE; POLYMERS; PROTEIN FIBERS; SILK;

EID: 78650693161     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201003795     Document Type: Article

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