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Subunit Structure and Conformation of Bombyx Mori Silk Proteins

Subunit Structure and Conformation of Bombyx Mori Silk Proteins
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摘要 Molecular weights of the silk fibroin were determined by polyacrylamide gel electrophoresis in the presence of so-didium dodecyl sulfate (SDS - PAGE): The silk fibroin molecule consisted of subunits a, b and c with molecular weights of 280 kD, 230 kD and 25 kD respectively, of which the b subunit was composed of two subunits e and f with molecular weights of 130 kD and 125 kD, respec-tively, connected by disulfide bonds. The conformation of silk fibroin and subunits was determinated by Raman spectroscopy and Large angle X - ray diffraction) LAXS. The native silk fibroin only contained a - helix and random coil, but there were three conformation such as random - coil.a - helix and β - sheet in the silk fibroin dissolved in KSCN solution and frozen at - 20 °C. This suggested that KSCN solution and - 20°C freezing action could lead to the conformational transi-tion from random - coil and a - helix to P - sheet. The a subunit mainly existed in β - sheet conformation, in con-trast, the c subunit was Molecular weights of the silk fibroin were determined by polyacrylamide gel electrophoresis in the presence of so-didium dodecyl sulfate (SDS - PAGE): The silk fibroin molecule consisted of subunits a, b and c with molecular weights of 280 kD, 230 kD and 25 kD respectively, of which the b subunit was composed of two subunits e and f with molecular weights of 130 kD and 125 kD, respec-tively, connected by disulfide bonds. The conformation of silk fibroin and subunits was determinated by Raman spectroscopy and Large angle X - ray diffraction) LAXS. The native silk fibroin only contained a - helix and random coil, but there were three conformation such as random - coil.a - helix and β - sheet in the silk fibroin dissolved in KSCN solution and frozen at - 20 °C. This suggested that KSCN solution and - 20°C freezing action could lead to the conformational transi-tion from random - coil and a - helix to P - sheet. The a subunit mainly existed in β - sheet conformation, in con-trast, the c subunit was chiefly in the form of a - helix conformation.
出处 《Journal of China Textile University(English Edition)》 EI CAS 1998年第4期6-9,共4页
基金 the Foundation of Hao Yingdong Youth Teacher and Shanghai Youth Scientific
关键词 SILK protein SUBUNIT CONFORMATION SDS -PAGE Raman spectroscopy LAXS silk protein, subunit, conformation, SDS -PAGE, Raman spectroscopy, LAXS
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