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Spectroscopic Study of Ser92 Mutants of Human Myoglobin:Hydrogen Bonding Effect of Ser92 to Proximal His93 on Structure and Property of Myoglobin
Carbon Monoxide Cyanides Escherichia coli Ferric Compounds Ferrous Compounds Histidine Humans Hydrogen Bonding Magnetic Resonance Spectroscopy Mutagenesis Myoglobin Myoglobin Oxygen Polymerase Chain Reaction Recombinant Fusion Proteins Serine Serine Spectrophotometr Spectrum Analysis, Raman Structure-Activity Relationship
2016/5/23
Neutron diffraction studies have demonstrated that the hydroxyl group oxygen of Ser92(F7) is hydrogen bonded to the proximal His93(48) N epsilon H proton in myoglobin (Mb) [Cheng, X., & Shoenborn, B. ...
Ultrafast Measurements of Geminate Recombination of NO with Site-specific Mutants of Human Myoglobin
human myoglobin mutagenesis kinetics structure-function relationships picosecond timescale
2016/5/23
Flash photolysis studies of NO recombination to heme proteins offer a direct probe of protein structural changes on the tens of picoseconds timescale where they can be compared with molecular dynamics...
Dynamics of Protein Relaxation in Site-Specific Mutants of Human Myoglobin
Humans Cysteine Heme Alanine Myoglobin Recombinant Proteins Spectrophotometry Mutagenesis,Site-Directed Amino Acid Sequence Protein Conformation
2016/5/23
We have recently reported spectroscopic evidence for structural relaxation of myoglobin (Mb) following photodissociation of MbCO [Lambright, D. G., Balasubramanian, S., & Boxer, S. G. (1991) Chem. Phy...
Perturbations of the Distal Heme Pocket in Human Myoglobin Mutants Probed by Infrared Spectroscopy of Bound CO:Correlation with Ligand Binding Kinetics
Distal Heme Pocket Human Myoglobin Mutants Probed Infrared Spectroscopy Bound CO:Correlation Ligand Binding Kinetics
2016/5/23
The infrared spectra of CO bound to human myoglobin and myoglobin mutants at positions His-64, Val-68, Asp-60, and Lys-45 on the distal side have been measured between 100 and 300 K. Large differences...
X-ray Crystal Structure of a Mutant Recombinant Human Myoglobin at 2.8Å Resolution
Humans Myoglobin Recombinant Proteins X-Ray Diffraction Protein Conformation Mutation Molecular Structure
2016/5/23
We have grown crystals in trigonal space group P 3 2 21 of a mutant human myoglobin, aquomet form, in which lysine at position 45 has been replaced by arginine and cysteine at position 110 has been re...