[NMR paper] Insights into the Structure of Invisible Conformations of Large Methyl Group Labeled Molecular Machines from High Pressure NMR
Insights into the Structure of Invisible Conformations of Large Methyl Group Labeled Molecular Machines from High Pressure NMR
Most proteins are highly flexible and can adopt conformations that deviate from the energetically most favorable ground state. Structural information on these lowly populated, alternative conformations is often lacking, despite the functional importance of these states. Here, we study the pathway by which the Dcp1:Dcp2 mRNA decapping complex exchanges between an autoinhibited closed and an open conformation. We make use of methyl Carr-Purcell-Meiboom-Gill (CPMG)...
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06-18-2023 07:41 PM
[NMR paper] Protein-Ligand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure
Protein-Ligand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure
Proteins undergo changes in their partial volumes in numerous biological processes such as enzymatic catalysis, unfolding-refolding, and ligand binding. The change in the protein volume upon ligand binding-a parameter termed the protein-ligand binding volume-can be extensively studied by high-pressure NMR spectroscopy. In this study, we developed a method to determine the protein-ligand binding volume from a single two-dimensional (2D) ¹H-^(15)N heteronuclear single quantum coherence (HSQC)...
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05-26-2021 12:50 PM
[NMR paper] Thermodynamic stability of hnRNP A1 low complexity domain revealed by high-pressure NMR.
Thermodynamic stability of hnRNP A1 low complexity domain revealed by high-pressure NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png Related Articles Thermodynamic stability of hnRNP A1 low complexity domain revealed by high-pressure NMR.
Proteins. 2021 Feb 06;:
Authors: Levengood JD, Peterson J, Tolbert BS, Roche J
Abstract
We have investigated the pressure- and temperature-induced conformational changes associated with the low complexity domain of...
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02-15-2021 01:33 PM
[NMR paper] Volume and Compressibility Differences Between Protein Conformations Revealed by High-Pressure NMR.
Volume and Compressibility Differences Between Protein Conformations Revealed by High-Pressure NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Volume and Compressibility Differences Between Protein Conformations Revealed by High-Pressure NMR.
Biophys J. 2021 Jan 29;:
Authors: Xu X, Gagné D, Aramini JM, Gardner KH
Abstract
Proteins often interconvert between different conformations in ways critical to their function. While manipulating...
[NMR paper] Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Related Articles Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Chembiochem. 2013 Jun 28;
Authors: Roche J, Ying J, Maltsev AS, Bax A
Abstract
The impact of pressure on the backbone (15) N, (1) H and (13) C chemical shifts in N-terminally acetylated ?-synuclein has been evaluated over a pressure range 1-2500 bar. Even while the chemical shifts fall very close...
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07-03-2013 01:46 PM
High-Pressure Protein Crystallography and NMR to Explore Protein Conformations.
High-Pressure Protein Crystallography and NMR to Explore Protein Conformations.
High-Pressure Protein Crystallography and NMR to Explore Protein Conformations.
Annu Rev Biophys. 2010 Jul 21;
Authors: Collins MD, Kim CU, Gruner SM
High-pressure methods for solving protein structures by X-ray crystallography and NMR are maturing. These techniques are beginning to impact our understanding of thermodynamic and structural features that define not only the protein's native conformation, but also the higher free energy conformations. The ability of...
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02-02-2011 02:40 AM
[NMR paper] Two folded conformers of ubiquitin revealed by high-pressure NMR.
Two folded conformers of ubiquitin revealed by high-pressure NMR.
Related Articles Two folded conformers of ubiquitin revealed by high-pressure NMR.
Biochemistry. 2001 Nov 13;40(45):13556-63
Authors: Kitahara R, Yamada H, Akasaka K
High-pressure 15N/1H two-dimensional NMR spectroscopy has been utilized to study conformational fluctuation of a 76-residue protein ubiquitin at pH 4.5 at 20 degrees C. The on-line variable pressure cell technique is used in conjunction with a high-field NMR spectrometer operating at 750 MHz for 1H in the pressure...
Volume and compressibility differences between protein conformations revealed by high-pressure NMR - ScienceDirect.com
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