NMR signal loss of mutant lysozyme with pressure [Biological Sciences]
NMR signal loss of mutant lysozyme with pressure
Kitahara, R., Mulder, F. A. A....
Date: 2015-03-03
In PNAS, Nucci et al. (1) present an NMR study suggesting the pressure-induced denaturation of individual domains of the T4 lysozyme mutant Leu99Ala (T4L L99A). The denaturation equilibrium was considered to be responsible for the pressure-induced loss of 15N-1H heteronuclear single quantum coherence (HSQC) cross-peaks, which were preferentially observed for... Read More
PNAS:
Number: 9
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03-03-2015 08:34 PM
[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...
Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant
Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant
September 2012
Publication year: 2012
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes, Volume 1818, Issue 9</br>
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Membrane proteins are vital for biological function, and their action is governed by structural properties critically depending on their interactions with the membranes. This has motivated considerable interest in studies of membrane protein folding and unfolding. Here the structural changes...
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02-03-2013 10:13 AM
[NMR paper] Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by m
Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR.
Related Articles Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR.
Biochemistry. 2000 Oct 17;39(41):12614-22
Authors: Mulder FA, Hon B, Muhandiram DR, Dahlquist FW, Kay LE
The Leu99-->Ala mutant of T4 lysozyme contains a large internal cavity in the core of its C-terminal domain that is capable of reversibly binding small hydrophobic compounds. Although the cavity is completely buried,...
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11-19-2010 08:29 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...
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[NMR paper] NMR study of the cold, heat, and pressure unfolding of ribonuclease A.
NMR study of the cold, heat, and pressure unfolding of ribonuclease A.
Related Articles NMR study of the cold, heat, and pressure unfolding of ribonuclease A.
Biochemistry. 1995 Jul 11;34(27):8631-41
Authors: Zhang J, Peng X, Jonas A, Jonas J
The reversible cold, heat, and pressure unfolding of RNase A and RNase A--inhibitor complex were studied by 1D and 2D 1H NMR spectroscopy. The reversible pressure denaturation experiments in the pressure range from 1 bar to 5 kbar were carried out at pH 2.0 and 10 degrees C. The cold denaturation was...
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[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...
Is pressure-induced signal loss in NMR spectra for the Leu99Ala cavity mutant of T4 lysozyme due to unfolding?
Linear Mode
