搜索结果: 1-4 共查到“生物化学 Hydrogen Bonding”相关记录4条 . 查询时间(0.12 秒)
Measuring Electrostatic Fields in Both Hydrogen Bonding and non-Hydrogen Bonding Environments using Carbonyl Vibrational Probes
Ribonucleases Molecular Probes Protein Conformation Vibration Acetophenones Molecular Dynamics Simulation Static Electricity Hydrogen Bonding Solvents
2016/5/25
Vibrational probes can provide a direct readout of the local electrostatic field in complex molecular environments, such as protein binding sites and enzyme active sites. This information provides an ...
Decomposition of Vibrational Shifts of Nitriles into Electrostatic and Hydrogen-Bonding Effects
Pseudomonas putida Nitriles Steroid Isomerases Spectrophotometry, Infrared Magnetic Resonance Spectroscopy Catalytic Domain Hydrogen Bonding Vibration Static Electricity
2016/5/25
Infrared (IR) band shifts of isolated vibrational transitions can serve as quantitative and directional probes of local electrostatic fields, due to the vibrational Stark effect. However, departures f...
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...
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. ...