Amplitude of Pancreatic Lipase Lid Opening in Solution and Identification of Spin Label Conformational Subensembles by Combining Continuous Wave and Pulsed EPR Spectroscopy and Molecular Dynamics

Biochemistry ◽  
2010 ◽  
Vol 49 (10) ◽  
pp. 2140-2149 ◽  
Author(s):  
Sebastien Ranaldi ◽  
Valérie Belle ◽  
Mireille Woudstra ◽  
Raphael Bourgeas ◽  
Bruno Guigliarelli ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Pancreatic Lipase ◽  
Epr Spectroscopy ◽  
Spin Label ◽  
Continuous Wave ◽  
Pulsed Epr

scholarly journals A Spirocyclohexyl Nitroxide Amino Acid Spin Label for Pulsed EPR Spectroscopy Distance Measurements

2010 ◽  
Vol 16 (19) ◽  
pp. 5778-5782 ◽  
Author(s):  
Andrzej Rajca ◽  
Velavan Kathirvelu ◽  
Sandip K. Roy ◽  
Maren Pink ◽  
Suchada Rajca ◽  
...  
Keyword(s):  
Amino Acid ◽  
Epr Spectroscopy ◽  
Spin Label ◽  
Distance Measurements ◽  
Pulsed Epr ◽  
Nitroxide Amino Acid

Long-range distance determinations in biomacromolecules by EPR spectroscopy

2007 ◽  
Vol 40 (1) ◽  
pp. 1-53 ◽  
Author(s):  
Olav Schiemann ◽  
Thomas F. Prisner
Keyword(s):  
Long Range ◽  
Epr Spectroscopy ◽  
Structural Changes ◽  
Continuous Wave ◽  
Double Resonance ◽  
Theoretical Background ◽  
Spin Labels ◽  
Paramagnetic Resonance ◽  
Pulsed Epr ◽  
Amino Acid Radicals

AbstractElectron paramagnetic resonance (EPR) spectroscopy provides a variety of tools to study structures and structural changes of large biomolecules or complexes thereof. In order to unravel secondary structure elements, domain arrangements or complex formation, continuous wave and pulsed EPR methods capable of measuring the magnetic dipole coupling between two unpaired electrons can be used to obtain long-range distance constraints on the nanometer scale. Such methods yield reliably and precisely distances of up to 80 Å, can be applied to biomolecules in aqueous buffer solutions or membranes, and are not size limited. They can be applied either at cryogenic or physiological temperatures and down to amounts of a few nanomoles. Spin centers may be metal ions, metal clusters, cofactor radicals, amino acid radicals, or spin labels. In this review, we discuss the advantages and limitations of the different EPR spectroscopic methods, briefly describe their theoretical background, and summarize important biological applications. The main focus of this article will be on pulsed EPR methods like pulsed electron–electron double resonance (PELDOR) and their applications to spin-labeled biosystems.

A semi-rigid isoindoline-derived nitroxide spin label for RNA

2018 ◽  
Vol 16 (5) ◽  
pp. 816-824 ◽  
Author(s):  
Dnyaneshwar B. Gophane ◽  
Burkhard Endeward ◽  
Thomas F. Prisner ◽  
Snorri Th. Sigurdsson
Keyword(s):  
Epr Spectroscopy ◽  
Spin Label ◽  
Spin Labels ◽  
Pulsed Epr ◽  
Rna Duplexes ◽  
Limited Motion

The new semi-rigid spin label ImUm showed limited motion in RNA duplexes and accurate distances between two spin labels in RNA duplexes were obtained by pulsed EPR spectroscopy.

scholarly journals Characterizing SPASM/twitch Domain-Containing Radical SAM Enzymes by EPR Spectroscopy

2021 ◽  
Author(s):  
Aidin R. Balo ◽  
Lizhi Tao ◽  
R. David Britt
Keyword(s):  
Epr Spectroscopy ◽  
Continuous Wave ◽  
Spectroscopic Studies ◽  
Paramagnetic Species ◽  
Paramagnetic Resonance ◽  
Iron Sulfur Cluster ◽  
Radical Sam Enzymes ◽  
Iron Sulfur ◽  
Pulse Epr ◽  
Multiple Domains

AbstractOwing to their importance, diversity and abundance of generated paramagnetic species, radical S-adenosylmethionine (rSAM) enzymes have become popular targets for electron paramagnetic resonance (EPR) spectroscopic studies. In contrast to prototypic single-domain and thus single-[4Fe–4S]-containing rSAM enzymes, there is a large subfamily of rSAM enzymes with multiple domains and one or two additional iron–sulfur cluster(s) called the SPASM/twitch domain-containing rSAM enzymes. EPR spectroscopy is a powerful tool that allows for the observation of the iron–sulfur clusters as well as potentially trappable paramagnetic reaction intermediates. Here, we review continuous-wave and pulse EPR spectroscopic studies of SPASM/twitch domain-containing rSAM enzymes. Among these enzymes, we will review in greater depth four well-studied enzymes, BtrN, MoaA, PqqE, and SuiB. Towards establishing a functional consensus of the additional architecture in these enzymes, we describe the commonalities between these enzymes as observed by EPR spectroscopy.

Sign in / Sign up

Export Citation Format

Share Document