PH-dependent dimerization of spider silk N-terminal domain requires relocation of a wedged tryptophan side chain

Journal of Molecular Biology

Volumn 422, Issue 4, 2012, Pages 477-487

  Jaudzems, Kristaps ^a   Askarieh, Glareh ^b   Landreh, Michael ^c   Nordling, Kerstin ^c   Hedhammar, My ^b   Jörnvall, Hans ^c   Rising, Anna ^b,c   Knight, Stefan D ^b   Johansson, Jan ^b,c,d  

^a LATVIAN INSTITUTE OF ORGANIC SYNTHESIS   (Latvia)

^b SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^c KAROLINSKA INSTITUTE   (Sweden)

^d TALLINN UNIVERSITY   (Estonia)

Author keywords

NMR structure; protein assembly; spidroin; X ray structure

Indexed keywords

DIMER; MONOMER; PROTEIN; SILK FIBROIN; SODIUM CHLORIDE; SPIDER SILK PROTEIN SPIDROIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; EUPROSTHENOPS AUSTRALIS; FLUORESCENCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN STRUCTURE; SILK; SPIDER;

ARANEAE; EUPROSTHENOPS;

EID: 84865523517     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.06.004     Document Type: Article

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