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搜索结果: 1-15 共查到Mutant相关记录76条 . 查询时间(0.062 秒)
Researchers from Harvard’s Stem Cell and Regenerative Biology (HSCRB)’s Zon lab have discovered a new mechanism that influences melanoma development, a finding that could have wide implications for pa...
For the last five years, Waring “Buck” Trible has been having the same dream. He’s in the lab using CRISPR to tweak the genes of a wild worker ant. And poof! Like a Formicidae fairy tale, the lowly la...
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...
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...
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...
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...
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...
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...
Recently, heme protein cavity mutants have been engineered in which the proximal coordinating amino acid has been replaced by a smaller, noncoordinating residue leaving a cavity that can be filled by ...
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...
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 ...
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...
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...

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