Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Kevin M. Bobofchak"'
Autor:
Agustin O. Pineda, Christodoulos S. Flordellis, F. Scott Mathews, Michael E. Maragoudakis, Nikos E. Tsopanoglou, M. E. Papaconstantinou, Christopher J. Carrell, Kevin M. Bobofchak, Enrico Di Cera
Publikováno v:
Journal of Biological Chemistry. 280:29393-29396
Previous studies have suggested that thrombin interacts with integrins in endothelial cells through its RGD (Arg-187, Gly-188, Asp-189) sequence. All existing crystal structures of thrombin show that most of this sequence is buried under the 220-loop
Publikováno v:
Journal of Biological Chemistry. 280:25644-25650
The oxyanion hole of serine proteases is formed by the backbone N atoms of the catalytic Ser-195 and Gly-193 and engages the backbone O atom of the P1 residue of substrate in an important H-bonding interaction. The energetic contribution of this inte
Autor:
Clara Fronticelli, Michael Karavitis, Maria Teresa Sanna, William S. Brinigar, Kevin M. Bobofchak
Publikováno v:
Biophysical Chemistry. 98:115-126
Previous studies on bovine hemoglobin (HbBv) have suggested amino acid substitutions, which might introduce into human hemoglobin (HbA) functional characteristics of HbBv, namely a low intrinsic oxygen affinity regulated by Cl(-). Accordingly, we hav
Publikováno v:
Biochimica et biophysica acta. 1784(10)
A series of cross-linking reagents with 4 to 7 carbons have been synthesized and used to modify human hemoglobin. The product yields and biochemical properties of these cross-linked hemoglobins are compared to those made with both longer and shorter
Publikováno v:
Proteins. 44(3)
We have engineered a recombinant mutant human hemoglobin, Hb Prisca β(S9C+C93A+C112G), which assembles in a polymeric form. The polymerization is obtained through the formation of intermolecular SS bonds between cysteine residues introduced at posit