An Alternative Method for Pucker Determination in Carbohydrates from Residual Dipolar Couplings: A Solution NMR Study of the Fructofuranosyl Ring of Sucrose

Journal of the American Chemical Society ◽

10.1021/ja010981v ◽

2002 ◽

Vol 124 (10) ◽

pp. 2358-2362 ◽

Cited By ~ 38

Author(s):

Darón I. Freedberg

Keyword(s):

Residual Dipolar Couplings ◽

Dipolar Couplings ◽

Solution Nmr ◽

Alternative Method ◽

Nmr Study

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Detecting Protein Kinase Recognition Modes of Calmodulin by Residual Dipolar Couplings in Solution NMR†

Biochemistry ◽

10.1021/bi0264162 ◽

2002 ◽

Vol 41 (43) ◽

pp. 12899-12906 ◽

Cited By ~ 25

Author(s):

Tapas K. Mal ◽

Nikolai R. Skrynnikov ◽

Kyoko L. Yap ◽

Lewis E. Kay ◽

Mitsuhiko Ikura

Keyword(s):

Protein Kinase ◽

Residual Dipolar Couplings ◽

Dipolar Couplings ◽

Solution Nmr

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Increasing the Accuracy of Solution NMR Structures of Membrane Proteins by Application of Residual Dipolar Couplings. High-Resolution Structure of Outer Membrane Protein A

Journal of the American Chemical Society ◽

10.1021/ja0608343 ◽

2006 ◽

Vol 128 (21) ◽

pp. 6947-6951 ◽

Cited By ~ 52

Author(s):

Tomasz Cierpicki ◽

Binyong Liang ◽

Lukas K. Tamm ◽

John H. Bushweller

Keyword(s):

High Resolution ◽

Membrane Protein ◽

Residual Dipolar Couplings ◽

Protein A ◽

Dipolar Couplings ◽

Solution Nmr ◽

Nmr Structures ◽

High Resolution Structure ◽

Outer Membrane Protein A ◽

Resolution Structure

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Structure and Orientation of Ligands Bound to Membrane Proteins Are Reflected by Residual Dipolar Couplings in Solution NMR Measurements

ChemBioChem ◽

10.1002/1439-7633(20021004)3:10<975::aid-cbic975>3.0.co;2-y ◽

2002 ◽

Vol 3 (10) ◽

pp. 975-980 ◽

Cited By ~ 14

Author(s):

Bernd W. Koenig

Keyword(s):

Membrane Proteins ◽

Residual Dipolar Couplings ◽

Dipolar Couplings ◽

Solution Nmr

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ChemInform Abstract: Structure and Orientation of Ligands Bound to Membrane Proteins Are Reflected by Residual Dipolar Couplings in Solution NMR Measurements

ChemInform ◽

10.1002/chin.200249277 ◽

2010 ◽

Vol 33 (49) ◽

pp. no-no

Author(s):

Bernd W. Koenig

Keyword(s):

Membrane Proteins ◽

Residual Dipolar Couplings ◽

Dipolar Couplings ◽

Solution Nmr ◽

Abstract Structure

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Solution NMR Experiment for Measurement of 15N–1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes

Journal of the American Chemical Society ◽

10.1021/jacs.5b07010 ◽

2015 ◽

Vol 137 (35) ◽

pp. 11242-11245 ◽

Cited By ~ 5

Author(s):

Alexander Eletsky ◽

Surya V.S.R.K. Pulavarti ◽

Victor Beaumont ◽

Paul Gollnick ◽

Thomas Szyperski

Keyword(s):

Residual Dipolar Couplings ◽

Dipolar Couplings ◽

Solution Nmr ◽

Supramolecular Complexes ◽

Large Proteins

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Use of Residual Dipolar Couplings in Structural Analysis of Protein-Ligand Complexes by Solution NMR Spectroscopy

Micro and Nano Technologies in Bioanalysis - Methods in Molecular Biology ◽

10.1007/978-1-59745-483-4_15 ◽

2009 ◽

pp. 231-252 ◽

Cited By ~ 4

Author(s):

Nitin U. Jain

Keyword(s):

Nmr Spectroscopy ◽

Structural Analysis ◽

Residual Dipolar Couplings ◽

Dipolar Couplings ◽

Solution Nmr ◽

Solution Nmr Spectroscopy

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Partial alignment, residual dipolar couplings and molecular symmetry in solution NMR

Journal of Biomolecular NMR ◽

10.1007/s10858-019-00256-2 ◽

2019 ◽

Vol 73 (8-9) ◽

pp. 477-491

Author(s):

Justin L. Lorieau

Keyword(s):

Residual Dipolar Couplings ◽

Dipolar Couplings ◽

Solution Nmr ◽

Molecular Symmetry ◽

Partial Alignment

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Faculty Opinions recommendation of Mg2+-induced variations in the conformation and dynamics of HIV-1 TAR RNA probed using NMR residual dipolar couplings.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1013337.192600 ◽

2003 ◽

Author(s):

Samuel Butcher

Keyword(s):

Residual Dipolar Couplings ◽

Dipolar Couplings ◽

Tar Rna ◽

Nmr Residual Dipolar Couplings ◽

Hiv 1

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Faculty Opinions recommendation of Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.12482956.13700054 ◽

2011 ◽

Author(s):

Vitali Tugarinov

Keyword(s):

Escherichia Coli ◽

Solution Structure ◽

Residual Dipolar Couplings ◽

Dipolar Couplings ◽

Wide Angle ◽

X Ray ◽

X Ray Scattering ◽

Enzyme I ◽

Ray Scattering

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Expression and Solution NMR Study of Multi-site Phosphomimetic Mutant BCL-2 Protein

Protein and Peptide Letters ◽

10.2174/0929866526666190327121225 ◽

2019 ◽

Vol 26 (6) ◽

pp. 449-457

Author(s):

Ting Song ◽

Keke Cao ◽

Yu dan Fan ◽

Zhichao Zhang ◽

Zong W. Guo ◽

...

Keyword(s):

Structural Change ◽

Structural Biology ◽

Quantum Coherence ◽

Structural Changes ◽

Solution Nmr ◽

Flexible Loop ◽

Loop Region ◽

Loop Domain ◽

Nmr Study ◽

Binding Groove

Background: The significance of multi-site phosphorylation of BCL-2 protein in the flexible loop domain remains controversial, in part due to the lack of structural biology studies of phosphorylated BCL-2. Objective: The purpose of the study is to explore the phosphorylation induced structural changes of BCL-2 protein. Methods: We constructed a phosphomietic mutant BCL-2(62-206) (t69e, s70e and s87e) (EEEBCL- 2-EK (62-206)), in which the BH4 domain and the part of loop region was truncated (residues 2-61) to enable a backbone resonance assignment. The phosphorylation-induced structural change was visualized by overlapping a well dispersed 15N-1H heteronuclear single quantum coherence (HSQC) NMR spectroscopy between EEE-BCL-2-EK (62-206) and BCL-2. Results: The EEE-BCL-2-EK (62-206) protein reproduced the biochemical and cellular activity of the native phosphorylated BCL-2 (pBCL-2), which was distinct from non-phosphorylated BCL-2 (npBCL-2) protein. Some residues in BH3 binding groove occurred chemical shift in the EEEBCL- 2-EK (62-206) spectrum, indicating that the phosphorylation in the loop region induces a structural change of active site. Conclusion: The phosphorylation of BCL-2 induced structural change in BH3 binding groove.

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