Zobrazeno 1 - 10
of 91
pro vyhledávání: '"R, Bogumil"'
Publikováno v:
Biochemistry. 34:10483-10490
The pH dependence of the electronic and EPR spectra of two variants of horse heart myoglobin (Mb) in which the distal His64 ligand has been replaced by either Thr or Ile has been studied. Both of these variants exhibit spectroscopic changes with pH t
Autor:
Gary D. Brayer, E Lloyd, Michael J. Smith, Robert Maurus, Mauk Ag, Hai-Lun Tang, R. Bogumil, Christie L. Hunter, H. Lee
Publikováno v:
Biochemistry. 33:7600-7608
The interaction of azide with variants of horse heart myoglobin (Mb) has been characterized by Fourier transform infrared (FTIR), electron paramagnetic resonance (EPR), and UV-VIS absorption spectroscopy and by molecular modeling calculations. Distal
The high-resolution X-ray crystallographic structures of horse heart azidometmyoglobin complexes of the wild-type protein and the His-64 → Thr variant have been determined to 2.0 and 1.8 Å respectively. Azide binds to wild-type metmyoglobin in a b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdf245bc62bda2d68ef237a59eb29efa
https://europepmc.org/articles/PMC1219452/
https://europepmc.org/articles/PMC1219452/
Autor:
Y. Luo, Christopher M. Overall, Mauk Ag, R. Bogumil, Robert Maurus, Gary D. Brayer, Michael Smith
Publikováno v:
Biochimica et biophysica acta. 1341(1)
Well-ordered internal amino acids can contribute significantly to the stability of proteins. To investigate the importance of the hydrophobic packing interface between helices G and H in the proximal heme pocket of horse heart myoglobin, the highly c
Publikováno v:
The Journal of biological chemistry. 269(17)
A site-specific mutant of horse heart myoglobin has been prepared in which the distal heme pocket residue, His64, is replaced by tyrosine. The structure of this myoglobin variant has been determined to 2.0-A resolution using x-ray diffraction techniq
Publikováno v:
Comparative biochemistry and physiology. B, Comparative biochemistry. 106(4)
1. A method developed for the isolation of phosvitin from chicken egg yolk was successfully applied to the isolation of phosvitin from salmon eggs. 2. Salmon roe phosvitin is smaller in molecular size than chicken egg phosvitin. 3. Circular dichroism
Akademický článek
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Publikováno v:
Journal of Inorganic Biochemistry. 51:95
Autor:
A.G. Mauk, Emma Lloyd, Hai-Lun Tang, Christopher M. Overall, D. P. Hildebrand, Michael J. Smith, R. Bogumil
Publikováno v:
Journal of Inorganic Biochemistry. 51:80
Akademický článek
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