Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Chuen-Shang C. Wu"'
Autor:
Tatsuya Samejima, Jen Tsi Yang, Hiroyuki Kaji, Chuen-Shang C. Wu, Keiichi Ando, Satoshi Koikeda, Kazunori Shiboya
Publikováno v:
Journal of Protein Chemistry. 13:307-313
The conformation of bilirubin oxidase (EC 1.3.3.5) from Myrothecium verrucaria was studied by circular dichroism (CD). The far-UV CD spectrum showed a single minimum at 215 nm and a maximum near 198 nm, suggesting the dominance of beta-sheets. There
Autor:
Chuen-Shang C. Wu, Richard D. Smith, Charles G. Edmonds, Joseph A. Loo, Karen J. Light-Wahl, H. Ewa Witkowska, Cedric H.L. Shackleton
Publikováno v:
Biological Mass Spectrometry. 22:112-120
Electrospray ionization collisionally activated dissociation (CAD) mass spectra of multiply charged human hemoglobin beta-chain variant proteins (146 amino acid residues, 15.9 kDa), generated in the atmospheric pressure/vacuum interface and in the co
Publikováno v:
Analytical Biochemistry. 200:359-364
The CD spectrum of certain all-β globular proteins resembles that of unfolded proteins with a characteristic negative band around 200 nm. The conformation of this class is tentatively termed β-II, which had two features that were absent for unfolde
Publikováno v:
Analytical Biochemistry. 198:250-255
The circular dichroic (CD) spectra of 16 reference proteins were analyzed by the Provencher-Glöckner method (Biochemistry 20, 31, 1981) with the lower-wavelength limit raised from 190 to 235 nm at 5-nm intervals. Fifty-one data points at 1-nm interv
Publikováno v:
Journal of Protein Chemistry. 10:427-436
The conformation of the 153-residue form of human basic fibroblast growth factor (bFGF) was studied with circular dichroism (CD) and sequence prediction methods. The far-UV CD spectrum with a minimum at 202 nm resembled that of an unordered polypepti
Publikováno v:
Biochimica et biophysica acta. 1162(1-2)
The hypoxanthine-guanine phosphoribosyltransferases (HGPRTases) of human and the parasitic trematode, Schistosoma mansoni, are of biomedical importance. The conformations of these two enzymes were studied by circular dichroism (CD). The schistosomal
Publikováno v:
Protein science : a publication of the Protein Society. 1(11)
The conformation of porcine serum ferric transferrin (Tf) and its stability against denaturation were studied by circular dichroism. Tf was estimated to have 19-24% alpha-helix and 50-55% beta-sheet based on the methods of Chang et al. (Chang, C.T.,
Publikováno v:
Journal of protein chemistry. 11(2)
The conformations of concanavalin A (con A), an all-β protein, and its three CNBr-cleaved fragments were studied by CD. Con A in buffer showed a 197 nm maximum and a 223 nm minimum, which were red-shifted by 6–7 nm from those of regular all-β pro
Publikováno v:
Journal of protein chemistry. 9(1)
The conformations of acetylcholine receptor from Torpedo californica in the absence and presence of agonists, antagonists, and local anesthetics were studied by circular dichroism (CD). Without ligands, the receptor had about 40% helix, 20% beta-shee
Autor:
Nancy M. Lee, Jen Tsi Yang, Andrew P. Smith, Horace H. Loh, Jun-Ichi Hasegawa, Chuen Shang C. Wu
Publikováno v:
Journal of protein chemistry. 9(1)
Based on circular dichroism (CD) and the sequence-predictive method, the opioid-binding cell adhesion molecule (OBCAM) consisted of one half beta-sheets and one fourth alpha-helices. This is consistent with significant sequence homology of the protei