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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. ...
Picosecond Spectroscopic Study of Chlorophyll-Based Models for the Primary Photochemistry of Photosynthesis
Picosecond Spectroscopic Study Chlorophyll-Based Models Primary Photochemistry Photosynthesis
2016/5/20
A series of covalently linked dimers and trimers of chlorophyllide derivatives was investigated by time-resolved absorption and fluorescence spectroscopy (3-lo4 ps). For these compounds, the freeenerg...