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Crystal Structure and Photodynamic Behavior of the Blue-emission Variant Y66H/Y145F of Green Fluorescent Protein
Animals Biological Transport Crystallography, X-Ray Green Fluorescent Proteins Hydrogen-Ion Concentration Luminescent Proteins Luminescent Proteins Luminescent Proteins Mutation Peptides Protein Folding Protons Scyphozoa Spectrometry,Fluorescence tructure-Activity Relationship Titrimetry
2016/5/23
The crystal structure of a blue emission variant (Y66H/Y145F) of the Aequorea victoria green fluorescent protein has been determined by molecular replacement and the model refined. The crystallographi...
Architecture and Function of Membrane Proteins in Planar Supported Bilayers:A Study with Photosynthetic Reaction Centers
Arabidopsis plant DNA repair photoreactivation plant blue-light receptor AT-PHH1
2016/5/23
We present a simple and convenient method for creating fluid supported bilayers which contain oriented and functional photosynthetic reaction centers (RCs). The supported bilayers are prepared by fusi...
Ultra-fast Excited State Dynamics in Green Fluorescent Protein:Multiple States and Proton Transfer
Protons Luminescent Proteins Green Fluorescent Proteins Recombinant Proteins Spectrometry, Fluorescence Temperature Amino Acid Sequence Protein Conformation Structure-Activity Relationship Oxidation-Reduction
2016/5/23
The green fluorescent protein (GFP) of the jellyfish Aequorea Victoria has attracted widespread interest since the discovery that its chromophore is generated by the autocatalytic, posttranslational c...
Vibrational Dynamics of Carbon Monoxide at the Active Sites of Mutant Heme Proteins
Vibrational Dynamics Carbon Monoxide Active Sites Mutant Heme Proteins
2016/5/23
Picosecond mid-IR pump−probe measurements of vibrational relaxation (VR) of CO bound to the active sites of wild-type and mutant myoglobins (Mb) reveal that an approximately linear relationship ...
Trans Effects in Nitric Oxide Binding to Myoglobin Cavity Mutant H93G
biology and medicine, basic studies nitric oxide biochemistry heme histidine imidazoles ligands mutants myoglobin proteins
2016/5/23
When nitric oxide (NO) binds to heme proteins, it exerts a repulsive trans effect on the proximal ligand, resulting in weakening or rupture of the proximal ligand-iron bond. The general question of wh...
Modulation of Protein Function by Exogenous Ligands in Protein Cavities:CO Binding to a Myoglobin Cavity Mutant Containing Unnatural Proximal Ligands
Animals Binding Sites Carbon Monoxide Cloning, Molecular Escherichia coli Heme Kinetics Ligands Magnetic Resonance Spectroscopy Mutagenesis, Site-Directed Myoglobin Myoglobin Point Mutation Protein Conformation ecombinant Proteins Recombinant Proteins Spectroscopy,Fourier Transform Infrared Valine Whales
2016/5/23
A variety of heterocyclic ligands can be exchanged into the proximal cavity of sperm whale myoglobin mutant H93G, providing a simple method for introduction of the equivalent of unnatural amino acid s...
A Test of the Role of Electrostatic Interactions in Determining the CO Stretch Frequency in Carbonmonoxymyoglobin
Electrochemistry Escherichia coli Humans Mutagenesis, Site-Directed Myoglobin Point Mutation Protein Conformation Recombinant Proteins Spectroscopy, Fourier Transform Infrared Vibration
2016/5/23
The vibrational frequency of CO bound to myoglobin can be varied by up to 60 cm-1 by making site-specific mutations in the distal pocket. These changes may result from specific chemical interactions b...
Functional Aspects of Ultra-rapid Heme Doming in Hemoglobin,Myoglobin,and the Myoglobin Mutant H93G
Animals Carboxyhemoglobin Carboxyhemoglobin Heme Hemoglobins Hemoglobins Horses Kinetics Myoglobin Myoglobin Myoglobin Point Mutation Spectrum Analysis, Raman Time Factors Whales
2016/5/23
Heme iron out-of-plane displacement following ligand dissociation in hemoglobin, myoglobin, and the proximal cavity mutant H93G is shown to be as rapid as the heme iron out-of-plane vibrational period...
Casting a Cold Eye over Myoglobin
Cold Temperature Crystallography,X-Ray Myoglobin Myoglobin Photolysis Protein Conformation
2016/5/23
Structural studies of carbonmonoxy myoglobin photolyzed at ultra-low temperatures have allowed the visualization of an otherwise elusive binding intermediate.
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. ...
Functional Cavities in Proteins:A General Method for Proximal Ligand Substitution in Myoglobin
Functional Cavities Proteins Proximal Ligand Substitution Myoglobin
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
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
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
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
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...