The catalytic cycle of Enzyme I (EI), a phosphotransferase enzyme responsible for converting phosphoenolpyruvate (PEP) into pyruvate, is characterized by a series of local and global conformational rearrangements. This multistep process includes a monomer-to-dimer transition, followed by an open-to-closed rearrangement of the dimeric complex upon PEP binding. In the present study, we investigate the thermodynamics of EI dimerization using a range of high-pressure solution NMR techniques...
[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] Probing the Transition State in Enzyme Catalysis by High-Pressure NMR Dynamics.
Probing the Transition State in Enzyme Catalysis by High-Pressure NMR Dynamics.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc-MS.gif Related Articles Probing the Transition State in Enzyme Catalysis by High-Pressure NMR Dynamics.
Nat Catal. 2019 Aug;2(8):726-734
Authors: Stiller JB, Kerns SJ, Hoemberger M, Cho YJ, Otten R, Hagan MF, Kern D
Abstract
Protein conformational changes are frequently essential for enzyme catalysis, and in several cases,...
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03-16-2020 04:59 PM
[NMR paper] Packing Arrangements and Inter-Sheet Interaction of Alanine Oligopeptides as Revealed by Relaxation Parameters Obtained From High-Resolution (13)C Solid-State NMR.
Packing Arrangements and Inter-Sheet Interaction of Alanine Oligopeptides as Revealed by Relaxation Parameters Obtained From High-Resolution (13)C Solid-State NMR.
Related Articles Packing Arrangements and Inter-Sheet Interaction of Alanine Oligopeptides as Revealed by Relaxation Parameters Obtained From High-Resolution (13)C Solid-State NMR.
J Phys Chem B. 2017 Sep 05;:
Authors: Naito A, Tasei Y, Nishimura A, Asakura T
Abstract
Alanine oligopeptides provide a key structure of the crystalline domains of the silks from spiders and...
[NMR paper] Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.
Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.
Related Articles Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.
Subcell Biochem. 2015;72:261-278
Authors: Roche J, Dellarole M, Royer CA, Roumestand C
Abstract
Defining the physical-chemical determinants of protein folding and stability, under normal and pathological conditions has constituted a major subfield in biophysical chemistry for over 50 years. Although a great deal of...
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07-16-2015 11:21 AM
[NMR paper] Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Biophys J. 2015 Jan 6;108(1):133-145
Authors: Maeno A, Sindhikara D, Hirata F, Otten R, Dahlquist FW, Yokoyama S, Akasaka K, Mulder FA, Kitahara R
Abstract
Although the structure, function, conformational dynamics, and controlled thermodynamics of proteins...
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01-08-2015 01:29 PM
[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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[NMR paper] Volumetric properties underlying ligand binding in a monomeric hemoglobin: A high-pressure NMR study.
Volumetric properties underlying ligand binding in a monomeric hemoglobin: A high-pressure NMR study.
Related Articles Volumetric properties underlying ligand binding in a monomeric hemoglobin: A high-pressure NMR study.
Biochim Biophys Acta. 2013 Apr 22;
Authors: Dellarole M, Roumestand C, Royer C, Lecomte JT
Abstract
The 2/2 hemoglobin of the cyanobacterium Synechococcus sp. PCC 7002, GlbN, coordinates the heme iron with two histidines and exists either with a b heme or with a covalently attached heme. The binding of exogenous ligands...
Elucidation of the mechanisms of inter-domain coupling in the monomeric state of Enzyme I by high-pressure NMR
Linear Mode
