Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Electron paramagnetic resonance spectroscopy site-directed

Lagerstedt, J.O., Budamagunta, M.S., Oda, M.N., and Voss, J.C. 2007. Electron paramagnetic resonance spectroscopy of site-directed spin labels reveals the structural heterogeneity in the N-terminal domain of ApoA-I in solution. The Journal of Biological Chemistry 282 9143-9149. [Pg.236]

Studying RNA Using Site-Directed Spin-Labeling and Continuous-Wave Electron Paramagnetic Resonance Spectroscopy... [Pg.303]

Based on work at the Max Planck Institute for Polymer Research [172, 173], pulsed electron paramagnetic resonance (EPR) has experienced a remarkable revival worldwide [174]. In particular, pulsed double electron-electron resonance (DEER) spectroscopy in combination with site-directed spin labeling [175] is extensively used today in studies of the structure of proteins, including their function as carriers of small molecules, and of nucleic acids. Moreover, it is used to probe large, complex biomacromolecules and their assemblies as weU as 1361 protein folding [176]. [Pg.168]

Eipper BA, Quon ASW, Mains RE, Boswell JS, Blackburn NJ. 1995. The catalytic core of peptidylglycine a-hydroxylating monooxygenase investigation by site-directed mutagenesis, Cu x-ray absorption spectroscopy, and electron paramagnetic resonance. Biochemistry 34 2857-2865. [Pg.502]

The technique of site-directed spin labeling (SDSL) provides information on bio-molecular systems by monitoring the behaviors of a stable radical tag (/.e spin label) using electron paramagnetic resonance (EPR) spectroscopy. SDSL studies of nucleic acids and protein-nucleic acid complexes have yielded unique information that is difficult to derive from other methods. In this chapter, we describe strategies used in nucleic acid SDSL investigations, and summarize advancements with a focus on those reported during the past five years. [Pg.122]

As well as oxidized enzyme states, a variety of reduced Mo(iv) and Mo(v) states are accessed during enzyme turnover or inhibition. Typically, Mo(vi) and Mo(iv) states are inter-converted by two-electron substrate transformations and Mo(v) states are generated during the first of the two sequential one-electron transfers required to regenerate the active site. Direct characterization of the diamagnetic, d, Mo(iv) states is limited but the paramagnetic, d, Mo(v) states have been extensively probed by EPR, Electron-Nuclear Double Resonance (ENDOR) and Magnetic Circular Dichroism (MCD) spectroscopies. " ... [Pg.211]


See other pages where Electron paramagnetic resonance spectroscopy site-directed is mentioned: [Pg.197]    [Pg.291]    [Pg.40]    [Pg.45]    [Pg.1384]    [Pg.237]    [Pg.553]    [Pg.118]    [Pg.195]    [Pg.372]    [Pg.28]    [Pg.13]    [Pg.303]    [Pg.287]    [Pg.112]    [Pg.237]    [Pg.536]    [Pg.91]    [Pg.92]    [Pg.520]    [Pg.82]    [Pg.179]    [Pg.273]    [Pg.145]    [Pg.122]    [Pg.19]    [Pg.46]    [Pg.213]    [Pg.925]    [Pg.6542]    [Pg.149]    [Pg.6541]    [Pg.20]   
See also in sourсe #XX -- [ Pg.526 ]




SEARCH



Electron directions

Electron paramagnetic

Electron paramagnetic resonance

Electron paramagnetic spectroscopy

Electron sites

Electronic paramagnetic resonance

Electrons resonance spectroscopy

Paramagnetic resonance

Paramagnetic resonance spectroscopy

Site-directed

© 2024 chempedia.info