scholarly journals Exact distance measurements for structure and dynamics in solid proteins by fast-magic-angle-spinning NMR

2019 ◽  
Vol 55 (55) ◽  
pp. 7899-7902 ◽  
Author(s):  
Kristof Grohe ◽  
Evgeny Nimerovsky ◽  
Himanshu Singh ◽  
Suresh K. Vasa ◽  
Benedikt Söldner ◽  
...  

With the integrative “eRFDR” approach, turning qualitative into exact distance restraints, high-resolution protein structures are obtained by fast-magic-angle-spinning solid-state NMR.

2017 ◽  
Vol 8 (11) ◽  
pp. 2399-2405 ◽  
Author(s):  
Mukul G. Jain ◽  
Daniela Lalli ◽  
Jan Stanek ◽  
Chandrakala Gowda ◽  
Satya Prakash ◽  
...  

2007 ◽  
Vol 40 (25) ◽  
pp. 9018-9025 ◽  
Author(s):  
Xiaoliang Wang ◽  
Qiang Gu ◽  
Qing Sun ◽  
Dongshan Zhou ◽  
Pingchuan Sun ◽  
...  

2011 ◽  
Vol 208 (1) ◽  
pp. 44-48 ◽  
Author(s):  
Yusuke Nishiyama ◽  
Yuki Endo ◽  
Takahiro Nemoto ◽  
Hiroaki Utsumi ◽  
Kazuo Yamauchi ◽  
...  

2021 ◽  
Vol 8 ◽  
Author(s):  
Patrick C. A. van der Wel

In structural studies of immobilized, aggregated and self-assembled biomolecules, solid-state NMR (ssNMR) spectroscopy can provide valuable high-resolution structural information. Among the structural restraints provided by magic angle spinning (MAS) ssNMR the canonical focus is on inter-atomic distance measurements. In the current review, we examine the utility of ssNMR measurements of angular constraints, as a complement to distance-based structure determination. The focus is on direct measurements of angular restraints via the judicious recoupling of multiple anisotropic ssNMR parameters, such as dipolar couplings and chemical shift anisotropies. Recent applications are highlighted, with a focus on studies of nanocrystalline polypeptides, aggregated peptides and proteins, receptor-substrate interactions, and small molecule interactions with amyloid protein fibrils. The review also examines considerations of when and where ssNMR torsion angle experiments are (most) effective, and discusses challenges and opportunities for future applications.


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