Characterization of Bifunctional Spin Labels for Investigating the Structural and Dynamic Properties of Membrane Proteins Using EPR Spectroscopy

2017 ◽  
Vol 121 (39) ◽  
pp. 9185-9195 ◽  
Author(s):  
Indra D. Sahu ◽  
Andrew F. Craig ◽  
Megan M. Dunagum ◽  
Robert M. McCarrick ◽  
Gary A. Lorigan
Keyword(s):  
Membrane Proteins ◽  
Epr Spectroscopy ◽  
Dynamic Properties ◽  
Spin Labels

scholarly journals Site-Directed Spin Labeling EPR for Studying Membrane Proteins

2018 ◽  
Vol 2018 ◽  
pp. 1-13 ◽  
Author(s):  
Indra D. Sahu ◽  
Gary A. Lorigan
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Membrane Proteins ◽  
Epr Spectroscopy ◽  
Dynamic Properties ◽  
Biological Systems ◽  
Spin Labeling ◽  
Paramagnetic Resonance ◽  
Site Directed Spin Labeling ◽  
Living Organisms ◽  
Electron Paramagnetic

Site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy is a rapidly expanding powerful biophysical technique to study the structural and dynamic properties of membrane proteins in a native environment. Membrane proteins are responsible for performing important functions in a wide variety of complicated biological systems that are responsible for the survival of living organisms. In this review, a brief introduction of the most popular SDSL EPR techniques and illustrations of recent applications for studying pertinent structural and dynamic properties on membrane proteins will be discussed.

scholarly journals Engineering nucleosomes for generating diverse chromatin assemblies

2021 ◽  
Author(s):  
Zenita Adhireksan ◽  
Deepti Sharma ◽  
Phoi Leng Lee ◽  
Qiuye Bao ◽  
Sivaraman Padavattan ◽  
...  
Keyword(s):  
Dynamic Properties ◽  
Dna Nanostructures ◽  
Macromolecular Assemblies ◽  
Maximum Resolution ◽  
Different Types ◽  
Chromatin Structural ◽  
Dna Fragment

Abstract Structural characterization of chromatin is challenging due to conformational and compositional heterogeneity in vivo and dynamic properties that limit achievable resolution in vitro. Although the maximum resolution for solving structures of large macromolecular assemblies by electron microscopy has recently undergone profound increases, X-ray crystallographic approaches may still offer advantages for certain systems. One such system is compact chromatin, wherein the crystalline state recapitulates the crowded molecular environment within the nucleus. Here we show that nucleosomal constructs with cohesive-ended DNA can be designed that assemble into different types of circular configurations or continuous fibers extending throughout crystals. We demonstrate the utility of the method for characterizing nucleosome compaction and linker histone binding at near-atomic resolution but also advance its application for tackling further problems in chromatin structural biology and for generating novel types of DNA nanostructures. We provide a library of cohesive-ended DNA fragment expression constructs and a strategy for engineering DNA-based nanomaterials with a seemingly vast potential variety of architectures and histone chemistries.

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