搜索结果: 16-30 共查到“理学 Myoglobin”相关记录33条 . 查询时间(0.022 秒)
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
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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. ...
Functional Cavities in Proteins:A General Method for Proximal Ligand Substitution in Myoglobin
Functional Cavities Proteins Proximal Ligand Substitution Myoglobin
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2016/5/23
Functional Cavities in Proteins:A General Method for Proximal Ligand Substitution in Myoglobin.
Determination of the Carbon Monoxide Binding Constants of Myoglobin Mutants:Comparison of Kinetic and Equilibrium Methods
Binding Sites Carbon Monoxide Humans Kinetics Mutagenesis, Site-Directed Mutation Myoglobin Myoglobin Myoglobin Nitric Oxide Photolysis Protein Conformation Spectroscopy, Fourier Transform Infrared Structure-Activity Relationship
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2016/5/23
The carbon monoxide (CO) binding constants of human myoglobin (Mb) and several single-site mutants have been determined using two different methods. In the kinetic method, which is commonly used for t...
Anatomy and Dynamics of a Ligand-Binding Pathway in Myoglobin:The Roles of Residues 45,60,64 and 68
Humans Carbon Monoxide Myoglobin Recombinant Proteins Ligands Spectrum Analysis Protein Binding Kinetics Mutation Thermodynamics
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2016/5/23
In order for diatomic ligands to enter and exit myoglobin, there must be substantial displacements of amino acid side chains from their positions in the static X-ray structure. One pathway, involving ...
Ultrafast Measurements of Geminate Recombination of NO with Site-specific Mutants of Human Myoglobin
human myoglobin mutagenesis kinetics structure-function relationships picosecond timescale
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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...
Discovery of New Ligand Binding Pathways in Myoglobin by Random Mutagenesis
Animals Whales Myoglobin Ligands Genetic Techniques Mutagenesis Binding Sites Amino Acid Sequence Protein Conformation Structure-Activity Relationship
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2016/5/23
A random library of single amino acid mutants of myoglobin was generated using a highly efficient, single-base-misincorporation random mutagenesis method to discover new ligand-binding pathways in myo...
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
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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
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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...
CO Recombination to Human Myoglobin Mutants in Glycerol-Water Solutions
CO Recombination Human Myoglobin Mutants Glycerol-Water Solutions
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2016/5/23
The kinetics of CO recombination to site-specific mutants of human myoglobin have been studied by flash photolysis in the temperature range 250-320 K on the nanosecond to second time scale in 75% glyc...
Protein Relaxation Dynamics in Human Myoglobin
Protein Relaxation Dynamics Human Myoglobin
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2016/5/23
Transient absorption spectra in the Soret region have been measured following the photolysis of human MbCO in 75%(w/w) glycerol:water at 250, 270, and 290 K. The peak of the transient difference spect...
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
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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...
Ligand and Proton Exchange Dynamics in Recombinant Human Myoglobin Mutants
Mb myoglobin n.m.r. nuclear magnetic resonance fwhm full width at half maximum TSP sodium 3-trimethyl silyl propionate DSS 4,4-dimethyl-4-sila pentane-1-sulfonate
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2016/5/20
Site-specific mutants of human myoglobin have been prepared in which lysine 45 is replaced by arginine (K45R) and aspartate 60 by glutamate (D60E), in order to examine the influence of these residues ...
Effects of Buried Ionizable Amino Acids on the Reduction Potential of Recombinant Myoglobin
Buried Ionizable Amino Acids Reduction Potential Recombinant Myoglobin
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2016/5/20
The temperature dependences of the reduction potentials (E degrees') of wild-type human myoglobin (Mb) and three site-directed mutants have been measured by the use of thin-layer spectroelectrochemist...
Effects of Dietary Chromium Methionine on Growth Performance, Carcass Composition, Meat Colour and Expression of the Colour-related Gene Myoglobin of Growing-finishing Pigs
Growing-finishing Pigs Chromium Methionine Meat Colour Myoglobin
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2016/5/12
To investigate the effect of dietary chromium (Cr) as Cr methionine (CrMet) on growth performance, carcass traits, pork quality, meat colour and expression of meat colour-related genes in growing-fini...
Skeletal Ryanodine Receptor 1-Heterozygous PSE (Pale, Soft and Exudative) Meat Contains a Higher Concentration of Myoglobin than Genetically Normal PSE Meat in Pigs
Meat Color Myoglobin PSE Pork Meat Skeletal Ryanodine Receptor 1-heterozygote
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2016/5/5
Comparisons of properties between skeletal ryanodine receptor 1 (sRyR1)-heterozygous-mutated and normal types of meat were carried out in pigs using PSE (pale, soft and exudative) meat found during th...