Authors: Hata K, Kono R, Fujisawa M, Kitahara R, Kamatari YO, Akasaka K, Xu Y
We have investigated the effect of pressure and temperature on the structural and thermodynamic stability of a protein dihydrofolate reductase from a deep-sea bacterium Moritella profunda in its folate-bound form in the pressure range between 3 and 375 MPa and the temperature range between -5 and 30 degrees C. The on-line cell variable pressure 1H NMR spectroscopy has been used to analyze the chemical shift and signal intensity in one-dimensional 1H NMR spectra. Thermodynamic analysis based on signal intensities from protons in the core part indicates that the thermodynamic stability of Moritella profunda DHFR is relatively low over the temperature range between -5 and 30 degrees C (deltaG0=15.8 +/- 4.1 kJ/mol at 15 degrees C), but is well adapted to the living environment of the bacterium (2 degrees C and 28 MPa), with the maximum stability around 5 degrees C (at 0.1 MPa) and a relatively small volume change upon unfolding (deltaV= 66 +/- 19 ml/mol). Despite the relatively low overall stability, the conformation in the core part of the folded protein remains intact up to approximately 200 MPa, showing marked stability of the core of this protein.
[NMR paper] High-pressure NMR study of the complex of a GTPase Rap1A with its effector RalGDS. A
High-pressure NMR study of the complex of a GTPase Rap1A with its effector RalGDS. A conformational switch in RalGDS revealed from non-linear pressure shifts.
Related Articles High-pressure NMR study of the complex of a GTPase Rap1A with its effector RalGDS. A conformational switch in RalGDS revealed from non-linear pressure shifts.
FEBS Lett. 2001 Oct 12;506(3):180-4
Authors: Inoue K, Maurer T, Yamada H, Herrmann C, Horn G, Kalbitzer HR, Akasaka K
Unusually large non-linear 1H and 15N nuclear magnetic resonance chemical shifts against...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] High pressure NMR study of a small protein, gurmarin.
High pressure NMR study of a small protein, gurmarin.
Related Articles High pressure NMR study of a small protein, gurmarin.
J Biomol NMR. 1998 Nov;12(4):535-41
Authors: Inoue K, Yamada H, Imoto T, Akasaka K
The effect of pressure on the structure of gurmarin, a globular, 35-residue protein from Gymnema sylvestre, was studied in aqueous environment (95% 1H2O/5% 2H2O, pH 2.0) with an on-line variable pressure NMR system operating at 750 MHz. Two-dimensional TOCSY and NOESY spectra were measured as functions of pressure between 1 and 2000 bar at...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Dynamics of trimethoprim bound to dihydrofolate reductase--a deuterium NMR study.
Dynamics of trimethoprim bound to dihydrofolate reductase--a deuterium NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Dynamics of trimethoprim bound to dihydrofolate reductase--a deuterium NMR study.
Solid State Nucl Magn Reson. 1996 Dec;7(3):193-201
Authors: Yang QX, Huang FY, Lin TH, Gelbaum L, Howell EE, Huang TH
We have employed deuterium NMR techniques to determine the dynamics of trimethoprim (TMP) in a binary complex with dihydrofolate reductase...
nmrlearner
Journal club
0
08-22-2010 02:20 PM
[NMR paper] Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton
Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR.
J Mol Biol. 1995 Jul 28;250(5):689-94
Authors: Yamaguchi T, Yamada H, Akasaka K
Thermodynamic stability of ribonuclease A (6.2 mM pH 1.0, 0.15 M KCl, in 2H2O) has been studied in the pressure range of 1 to 2000 atm and in the temperature range...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
[NMR paper] High-resolution NMR study of the pressure-induced unfolding of lysozyme.
High-resolution NMR study of the pressure-induced unfolding of lysozyme.
Related Articles High-resolution NMR study of the pressure-induced unfolding of lysozyme.
Biochemistry. 1992 Sep 1;31(34):7773-8
Authors: Samarasinghe SD, Campbell DM, Jonas A, Jonas J
The pressure-induced reversible unfolding of lysozyme was investigated by high-resolution proton magnetic resonance spectroscopy by following the proton spectra of the following residues: His-15 epsilon 1, Trp-28 epsilon 3, Leu-17 delta 2, Cys-64 alpha, and Trp-108 epsilon 3. The...
nmrlearner
Journal club
0
08-21-2010 11:45 PM
[NMR paper] Dihydrofolate reductase: sequential resonance assignments using 2D and 3D NMR and sec
Dihydrofolate reductase: sequential resonance assignments using 2D and 3D NMR and secondary structure determination in solution.
Related Articles Dihydrofolate reductase: sequential resonance assignments using 2D and 3D NMR and secondary structure determination in solution.
Biochemistry. 1991 Jun 25;30(25):6330-41
Authors: Carr MD, Birdsall B, Frenkiel TA, Bauer CJ, Jimenez-Barbero J, Polshakov VI, McCormick JE, Roberts GC, Feeney J
Three-dimensional (3D) heteronuclear NMR techniques have been used to make sequential 1H and 15N resonance...
nmrlearner
Journal club
0
08-21-2010 11:16 PM
[NMR paper] The conformations of trimethoprim/E. coli dihydrofolate reductase complexes. A 15N an
The conformations of trimethoprim/E. coli dihydrofolate reductase complexes. A 15N and 31P NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The conformations of trimethoprim/E. coli dihydrofolate reductase complexes. A 15N and 31P NMR study.
FEBS Lett. 1991 May 20;283(1):44-6
Authors: Huang FY, Yang QX, Huang TH, Gelbaum L, Kuyper LF
We have employed 15N and 31P NMR techniques to characterize the conformations of trimethoprim (TMP)/E. coli dihydrofolate...
nmrlearner
Journal club
0
08-21-2010 11:16 PM
[NMR paper] NMR studies of interactions of ligands with dihydrofolate reductase.
NMR studies of interactions of ligands with dihydrofolate reductase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of interactions of ligands with dihydrofolate reductase.
Biochem Pharmacol. 1990 Jul 1;40(1):141-52
Authors: Feeney J
NMR spectroscopy is a useful technique for studying interactions, conformations and dynamic processes within ligand-protein complexes. Several examples of the application of the method to studies of complexes of anti-folate...