[NMR paper] High Pressure NMR Spectroscopy.
High Pressure NMR Spectroscopy.
Related Articles High Pressure NMR Spectroscopy.
Subcell Biochem. 2015;72:707-721
Authors: Akasaka K
Abstract
The combination of high-resolution NMR spectroscopy with pressure perturbation, known as variable-pressure NMR spectroscopy or simply high pressure NMR spectroscopy, is a relatively recent accomplishment, but is a technique expanding rapidly with high promise in future. The importance of the method is that it allows, for the first time in history, a systematic means of detecting and...
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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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07-03-2013 01:46 PM
[NMR images] High pressure NMR spectroscopy
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1/11/2010 8:48:44 AM GMT
High pressure NMR spectroscopy
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11-01-2010 09:23 AM
[NMR paper] Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of
Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.
J Mol Biol. 1996 Jun 21;259(4):805-18
Authors: Wong KB, Freund SM, Fersht AR
Detection of residual structure in denatured proteins is of interest because fleetingly structured regions may be initiation points of the...
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08-22-2010 02:27 PM
[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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08-22-2010 03:50 AM
[NMR paper] Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H N
Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Related Articles Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Biochemistry. 1991 Nov 26;30(47):11313-20
Authors: Tamura A, Kimura K, Akasaka K
Structural transitions of the protein Streptomyces subtilisin inhibitor (SSI) from the native state to the cold-denatured and heat-denatured states were studied by 1H NMR spectroscopy in the temperature range from -10 to 60 degrees C in the acidic pH range....
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08-21-2010 11:12 PM
[NMR paper] Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H N
Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Related Articles Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Biochemistry. 1991 Nov 26;30(47):11313-20
Authors: Tamura A, Kimura K, Akasaka K
Structural transitions of the protein Streptomyces subtilisin inhibitor (SSI) from the native state to the cold-denatured and heat-denatured states were studied by 1H NMR spectroscopy in the temperature range from -10 to 60 degrees C in the acidic pH range....
High-pressure and cold denaturation
Linear Mode
