The resonance frequency of an electron is highly sensitive to the
local magnetic field at the electron and can therefore be used as a
probe of the electron\'s direct surroundings. Electron Paramagnetic
Resonance (EPR or ESR) is a method by which this can be studied.
The presence of a nearby electron B may cause faster relaxation of
electron A, which depends on the distance between the two
electrons. Performing EPR relaxation measurements at high magnetic
fields (6.4 Tesla) provides the spectral resolution from which one
can extract information about the distance between and orientation
of electrons A and B with respect to each other. High-field EPR
relaxation measurements have been performed on the
electron-transfer proteins cytochrome c and cytochrome c oxidase.
These proteins form a short-lived complex in which an electron is
transferred from cytochrome c to its partner. The goal was to
determine the structure of this transient complex. Based on
extensive analysis and simulation of the data from conventional as
well as high-field EPR it is proposed in this work that the two
proteins do not build a single, well-defined complex, but rather
form unspecific, short-lived complexes.
VDM Verlag Dr. Mueller E.K.
|Country of origin:
Marloes Penning De Vries
||229 x 152 x 8mm (L x W x T)
||Paperback - Trade
Science & Mathematics >
Is the information for this product incomplete, wrong or inappropriate?
Let us know about it.
Does this product have an incorrect or missing image?
Send us a new image.
Is this product missing categories?
Add more categories.
Review This Product
No reviews yet - be the first to create one!