Characterization of recombinantly produced spider flagelliform silk domains

Journal of Structural Biology

Volumn 170, Issue 2, 2010, Pages 420-425

  Heim, Markus ^a   Ackerschott, Christian B ^b,c   Scheibel, Thomas ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^c Wyatt Technology Europe GmbH   (Germany)

Author keywords

Disulphide formation; Engineered spider silk; Protein folding; Protein oligomerization; Spider silk protein assembly; Spider silk protein solubility

Indexed keywords

PROTEIN; RECOMBINANT PROTEIN; SILK PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ELASTICITY; MOLECULAR WEIGHT; PREY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DOMAIN; SILK; SPIDER; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; CIRCULAR DICHROISM; DISULFIDES; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; SILK; SPIDERS;

ARANEAE;

EID: 77951977674     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.12.025     Document Type: Article

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