Identifying Protein Conformational Dynamics Using Spin‐label ESR

2019 ◽  
Vol 14 (22) ◽  
pp. 3981-3991 ◽  
Author(s):  
Yei‐Chen Lai ◽  
Yun‐Hsuan Kuo ◽  
Yun‐Wei Chiang
Keyword(s):  
Spin Label ◽  
Conformational Dynamics ◽  
Protein Conformational Dynamics

scholarly journals High-resolution EPR distance measurements on RNA and DNA with the non-covalent Ǵ spin label

2019 ◽  
Vol 48 (2) ◽  
pp. 924-933 ◽  
Author(s):  
Marcel Heinz ◽  
Nicole Erlenbach ◽  
Lukas S Stelzl ◽  
Grace Thierolf ◽  
Nilesh R Kamble ◽  
...  
Keyword(s):  
High Resolution ◽  
Nucleic Acids ◽  
Spin Label ◽  
Double Resonance ◽  
Conformational Dynamics ◽  
Md Simulations ◽  
Spin Labels ◽  
Abasic Site ◽  
Abasic Sites ◽  
Rna And Dna

Abstract Pulsed electron paramagnetic resonance (EPR) experiments, among them most prominently pulsed electron-electron double resonance experiments (PELDOR/DEER), resolve the conformational dynamics of nucleic acids with high resolution. The wide application of these powerful experiments is limited by the synthetic complexity of some of the best-performing spin labels. The recently developed $\bf\acute{G}$ (G-spin) label, an isoindoline-nitroxide derivative of guanine, can be incorporated non-covalently into DNA and RNA duplexes via Watson-Crick base pairing in an abasic site. We used PELDOR and molecular dynamics (MD) simulations to characterize $\bf\acute{G}$, obtaining excellent agreement between experiments and time traces calculated from MD simulations of RNA and DNA double helices with explicitly modeled $\bf\acute{G}$ bound in two abasic sites. The MD simulations reveal stable hydrogen bonds between the spin labels and the paired cytosines. The abasic sites do not significantly perturb the helical structure. $\bf\acute{G}$ remains rigidly bound to helical RNA and DNA. The distance distributions between the two bound $\bf\acute{G}$ labels are not substantially broadened by spin-label motions in the abasic site and agree well between experiment and MD. $\bf\acute{G}$ and similar non-covalently attached spin labels promise high-quality distance and orientation information, also of complexes of nucleic acids and proteins.

scholarly journals Protein Conformational Dynamics of Homodimeric Hemoglobin Revealed by Combined Time-Resolved Spectroscopic Probes

ChemPhysChem ◽  
2010 ◽  
Vol 11 (1) ◽  
pp. 109-114 ◽  
Author(s):  
Jungkweon Choi ◽  
Srinivasan Muniyappan ◽  
John T. Wallis ◽  
William E. Royer ◽  
Hyotcherl Ihee
Keyword(s):  
Conformational Dynamics ◽  
Time Resolved ◽  
Protein Conformational Dynamics ◽  
Spectroscopic Probes
Sign in / Sign up

Export Citation Format

Share Document