Theory
Article Abstract:
A study was conducted to describe an analytical model designed to characterize the coupling of protein fluctuations to electron transfer. The protein molecule was characterized by explicit atoms with fluctuations modeled by normal mode analysis. The electron transfer process was supported by the relaxation of nuclear coordinates surrounding the red-ox sites. Experimental results indicated that the model can quantitatively connect collective protein fluctuations to electron transfer.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1998
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Ultrafast phase grating studies of heme proteins: observation of the low-frequency modes directing functionally important protein motions
Article Abstract:
A study was conducted to analyze the tertiary global protein motions associated with the ligand to deligated conformation transition of carboxymyoglobin from 100 fs t0 2 ns. Transient phase grating spectroscopy was utilized to examine the motions. A mode-locked and Q-switched Nd3+:YAG laser was then utilized to determine the probe wavelength dependence of the protein acoustics. Results indicated that protein relaxation extends over several decades in time.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1998
User Contributions:
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