scholarly journals A New Labeling Method for Methyl Transverse Relaxation-Optimized Spectroscopy NMR Spectra of Alanine Residues

2007 ◽  
Vol 129 (50) ◽  
pp. 15428-15429 ◽  
Author(s):  
Rivka L. Isaacson ◽  
Peter J. Simpson ◽  
Minhao Liu ◽  
Ernesto Cota ◽  
Xiaodong Zhang ◽  
...  
Keyword(s):  
Nmr Spectra ◽  
Transverse Relaxation ◽  
Transverse Relaxation Optimized Spectroscopy ◽  
Labeling Method

Elimination of dispersion-components from high resolution NMR spectra and transverse relaxation times measurement

1997 ◽  
Vol 94 ◽  
pp. 1715-1725
Author(s):  
L Mahi ◽  
JC Duplan ◽  
A Briguet
Keyword(s):  
High Resolution ◽  
Nmr Spectra ◽  
Relaxation Times ◽  
Transverse Relaxation ◽  
High Resolution Nmr

scholarly journals Two-field transverse relaxation-optimized spectroscopy for the study of large biomolecules – An in silico investigation

2020 ◽  
Vol 4-5 ◽  
pp. 100007
Author(s):  
Nicolas Bolik-Coulon ◽  
Philippe Pelupessy ◽  
Guillaume Bouvignies ◽  
Fabien Ferrage
Keyword(s):  
In Silico ◽  
Transverse Relaxation ◽  
Transverse Relaxation Optimized Spectroscopy

scholarly journals Structural Model of the Fe-Hydrogenase/Cytochromec553Complex Combining Transverse Relaxation-optimized Spectroscopy Experiments and Soft Docking Calculations

2000 ◽  
Vol 275 (30) ◽  
pp. 23204-23210 ◽  
Author(s):  
Xavier Morelli ◽  
Mirjam Czjzek ◽  
Claude E. Hatchikian ◽  
Olivier Bornet ◽  
Juan C. Fontecilla-Camps ◽  
...  
Keyword(s):  
Structural Model ◽  
Transverse Relaxation ◽  
Docking Calculations ◽  
Transverse Relaxation Optimized Spectroscopy ◽  
Soft Docking

Transverse relaxation effects resulting from deuterium exchange in the proton NMR spectra of proteins

1980 ◽  
Vol 37 (1) ◽  
pp. 141-153
Author(s):  
R Cassels ◽  
C.M Dobson ◽  
F.M Poulsen ◽  
R.G Ratcliffe ◽  
R.J.P Williams
Keyword(s):  
Nmr Spectra ◽  
Proton Nmr ◽  
Deuterium Exchange ◽  
Transverse Relaxation ◽  
Relaxation Effects

scholarly journals NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy

1998 ◽  
Vol 95 (24) ◽  
pp. 14147-14151 ◽  
Author(s):  
K. Pervushin ◽  
A. Ono ◽  
C. Fernandez ◽  
T. Szyperski ◽  
M. Kainosho ◽  
...  
Keyword(s):  
Hydrogen Bonds ◽  
Base Pair ◽  
Scalar Couplings ◽  
Transverse Relaxation ◽  
Transverse Relaxation Optimized Spectroscopy

scholarly journals Exploring long-range cooperativity in the 20S proteasome core particle from Thermoplasma acidophilum using methyl-TROSY–based NMR

2020 ◽  
Vol 117 (10) ◽  
pp. 5298-5309
Author(s):  
Enrico Rennella ◽  
Rui Huang ◽  
Zanlin Yu ◽  
Lewis E. Kay
Keyword(s):  
Molecular Machines ◽  
Molecular Assembly ◽  
20S Proteasome ◽  
Core Particle ◽  
Thermoplasma Acidophilum ◽  
Transverse Relaxation ◽  
Catalytic Sites ◽  
Methyl Trosy ◽  
Transverse Relaxation Optimized Spectroscopy ◽  
Allosteric Pathway

The 20S core particle (CP) proteasome is a molecular assembly catalyzing the degradation of misfolded proteins or proteins no longer required for function. It is composed of four stacked heptameric rings that form a barrel-like structure, sequestering proteolytic sites inside its lumen. Proteasome function is regulated by gates derived from the termini of α-rings and through binding of regulatory particles (RPs) to one or both ends of the barrel. The CP is dynamic, with an extensive allosteric pathway extending from one end of the molecule to catalytic sites in its center. Here, using methyl-transverse relaxation optimized spectroscopy (TROSY)-based NMR optimized for studies of high–molecular-weight complexes, we evaluate whether the pathway extends over the entire 150-Å length of the molecule. By exploiting a number of different labeling schemes, the two halves of the molecule can be distinguished, so that the effects of 11S RP binding, or the introduction of gate or allosteric pathway mutations at one end of the barrel can be evaluated at the distal end. Our results establish that while 11S binding and the introduction of key mutations affect each half of the CP allosterically, they do not further couple opposite ends of the molecule. This may have implications for the function of so-called “hybrid” proteasomes where each end of the CP is bound with a different regulator, allowing the CP to be responsive to both RPs simultaneously. The methodology presented introduces a general NMR strategy for dissecting pathways of communication in homo-oligomeric molecular machines.

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