Determination of High-resolution NMR Structures of Proteins

1993 ◽  
pp. 53-91 ◽  
Author(s):  
David A. Case ◽  
Peter E. Wright
Keyword(s):  
High Resolution ◽  
Nmr Structures ◽  
High Resolution Nmr ◽  
Nmr Structures Of Proteins

Determination of Tautomeric Preference of Fenobam in Solution by High Resolution NMR Spectroscopy

2020 ◽  
Author(s):  
Xuming Sha ◽  
Shaodong Chen ◽  
Xiaojing Zheng ◽  
Xin Ye ◽  
Hailu Zhang ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
High Resolution ◽  
High Resolution Nmr

scholarly journals High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins

2016 ◽  
Vol 55 (35) ◽  
pp. 10518-10521 ◽  
Author(s):  
Mariusz Jaremko ◽  
Łukasz Jaremko ◽  
Saskia Villinger ◽  
Christian D. Schmidt ◽  
Christian Griesinger ◽  
...  
Keyword(s):  
High Resolution ◽  
Membrane Proteins ◽  
Dynamic Structure ◽  
High Resolution Nmr

Elucidation of Polymer Microstructure by High Resolution NMR Spectroscopy

1967 ◽  
Vol 40 (2) ◽  
pp. 385-399 ◽  
Author(s):  
Raymond C. Ferguson
Keyword(s):  
Nmr Spectroscopy ◽  
High Resolution ◽  
Spectral Data ◽  
High Field ◽  
Structural Features ◽  
Polymer Microstructure ◽  
Structural Isomerism ◽  
High Resolution Nmr ◽  
Polymer Tacticity

Abstract High resolution NMR spectroscopy is proving to be a useful experimental technique for determining the microstructures of high polymers. Its major utility, aside from identifying structural features often not detectable by other methods, lies in quantitative applications. Some examples are the determination of monomer ratios in copolymers, polymer tacticity, sequence isomerism of monomer units, and other types of structural isomerism. The applicability of the method is being enhanced by continuing development of high-field spectrometers, special accessories, and new experimental techniques, and by application of computers to the analysis of spectral data.

Author response for "Determination of Tautomeric Preference of Fenobam in Solution by High Resolution NMR Spectroscopy"

2020 ◽  
Author(s):  
Xuming Sha ◽  
Shaodong Chen ◽  
Xiaojing Zheng ◽  
Xin Ye ◽  
Hailu Zhang ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
High Resolution ◽  
Author Response ◽  
High Resolution Nmr

scholarly journals High-resolution NMR structures of the domains ofSaccharomyces cerevisiaeTho1

2016 ◽  
Vol 72 (6) ◽  
pp. 500-506
Author(s):  
Julian O. B. Jacobsen ◽  
Mark D. Allen ◽  
Stefan M. V. Freund ◽  
Mark Bycroft
Keyword(s):  
High Resolution ◽  
Rna Binding ◽  
Mrna Processing ◽  
Dependent Manner ◽  
Nmr Structures ◽  
High Resolution Nmr ◽  
N Terminus ◽  
Resolution Structure

THO is a multi-protein complex involved in the formation of messenger ribonuclear particles (mRNPs) by coupling transcription with mRNA processing and export. THO is thought to be formed from five subunits, Tho2p, Hpr1p, Tex1p, Mft1p and Thp2p, and recent work has determined a low-resolution structure of the complex [Poulsenet al.(2014),PLoS One,9, e103470]. A number of additional proteins are thought to be involved in the formation of mRNP in yeast, including Tho1, which has been shown to bind RNAin vitroand is recruited to actively transcribed chromatinin vivoin a THO-complex and RNA-dependent manner. Tho1 is known to contain a SAP domain at the N-terminus, but the ability to suppress the expression defects of thehpr1Δ mutant of THO was shown to reside in the RNA-binding C-terminal region. In this study, high-resolution structures of both the N-terminal DNA-binding SAP domain and C-terminal RNA-binding domain have been determined.

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