Self-assembly of spider silk proteins is controlled by a pH-sensitive relay

Nature

Volumn 465, Issue 7295, 2010, Pages 236-238

  Askarieh, Glareh ^a,b   Hedhammar, My ^b   Nordling, Kerstin ^b   Saenz, Alejandra ^c   Casals, Cristina ^c   Rising, Anna ^b   Johansson, Jan ^b   Knight, Stefan D ^b  

^a UNIVERSITY OF OSLO   (Norway)

^b UPPSALA UNIVERSITY   (Sweden)

^c UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

AMPULLATE SPIDROIN 1 PROTEIN; INSECT PROTEIN; PROTEIN; SILK PROTEIN; UNCLASSIFIED DRUG;

ELASTICITY; PH; POLYMER; PROTEIN; RESOLUTION; SHEAR STRESS; SPIDER;

AMINO TERMINAL SEQUENCE; ARTICLE; COMPETITIVE INHIBITION; CONTROLLED STUDY; EUPROSTHENOPS AUSTRALIS; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN STRUCTURE; REGULATORY MECHANISM; SILK; SPIDER; STRUCTURE ANALYSIS; X RAY ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; CIRCULAR DICHROISM; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SILK; SPIDERS; STATIC ELECTRICITY;

ARANEAE; EUPROSTHENOPS; PISAURIDAE;

EID: 77952337074     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08962     Document Type: Article

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