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A Whole-Genome Sequenced Rice Mutant Resource for the Study of Biofuel Feedstocks
Whole-Genome Sequenced Rice Mutant Resource Biofuel Feedstocks
2017/7/24
Rice is a staple food for over half of the world’s population and a model for studies of candidate bioenergy grasses such as sorghum, switchgrass, and Miscanthus. To optimize crops for biofu...
Fine-tuning dosage of mutant genes unleashes long-trapped yield potential in tomato plants(图)
Fine-tuning dosage mutant genes unleashes long-trapped tomato plants
2017/7/20
Breeding in plants and animals typically involves straightforward addition. As beneficial new traits are discovered—like resistance to drought or larger fruits—they are added to existing prized variet...
As we push the limits of agriculture to feed more people in a warmer world, we do not understand how plants sense temperature.In a surprising turn of events, scientists at the University of Buenos Air...
Charge Delocalization in the Special-Pair Radical Cation of Mutant Reaction Centers of Rhodobacter Sphaeroides from Stark Spectra and Nonadiabatic Spectral Simulations
Rhodobacter sphaeroides Cations Spectrophotometry Spectroscopy, Fourier Transform Infrared Mutagenesis,Site-Directed Absorption Dimerization Oxidation-Reduction Mutation Electrochemistry
2016/5/24
Stark and absorption spectra for the hole-transfer band of the bacteriochlorophyll special pair in the wild-type and L131LH, M160LH, and L131LH/M160LH mutants of the bacterial reaction center of Rhodo...
19F NMR of Trifluoroacetyl-Labeled Cysteine Mutants of Myoglobin:Structural Probes of Nitric Oxide Bound to the H93G Cavity Mutant
19F NMR Trifluoroacetyl Cysteine Mutants Myoglobin Nitric Oxide H93G Cavity Mutant
2016/5/23
Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a 5- or 6-coordinate Fe--NO heme complex. The H93G mutation replaces the proximal histidine of Mb with glycine, allowi...
Excited State Energy Transfer Pathways in Photosynthetic Reaction Centers.4.Asymmetric Energy Transfer in the Heterodimer Mutant
in-modified beta zeolite reductive solid-state ion exchange Lewis acidity m-xylene transformation
2016/5/23
In bacterial photosynthetic reaction centers, ultrafast singlet excited state energy transfer occurs from the monomeric bacteriochlorophylls, B, and bacteriopheophytins, H, to the homodimer special pa...
The H93G Myoglobin Cavity Mutant as a Versatile Template for Modeling Heme Proteins:Ferrous,Ferric,and Ferryl Mixed-Ligand Complexes with Imidazole in the Cavity
copper(II) azomethine imidate crystal structures
2016/5/23
One of the difficulties in preparing accurate ambient-temperature model complexes for heme proteins, particularly in the ferric state, has been the generation of mixed-ligand adducts: complexes with d...
The Role of the Distal and Proximal Protein Environments in Controlling the Ferric Spin State and in Stabilizing Thiolate Ligation in Heme Systems:Thiolate Adducts of the Myoglobin H93G Cavity Mutant
salicylic alcohols hydrogen bonds quantum chemistry
2016/5/23
Recently, heme protein cavity mutants have been engineered in which the proximal coordinating amino acid has been replaced by a smaller, noncoordinating residue leaving a cavity that can be filled by ...
Hydrogen Bonding Modulates Binding of Exogenous Ligands in a Myoglobin Proximal Cavity Mutant
Alanine Amino Acid Substitution Animals Binding Sites Glycine Histidine Hydrogen Bonding Imidazoles Ligands Macromolecular Substances Metmyoglobin Models, Chemical Mutagenesis, Insertional Myoglobin Nitric Oxide Nuclear Magnetic Resonance,Biomolecular Protons Serine Threonine Whales
2016/5/23
In the sperm whale myoglobin mutant H93G, the proximal histidine is replaced by glycine, leaving a cavity in which exogenous imidazole can bind and ligate the heme iron (Barrick, D. (1994) Biochemistr...
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...
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...