[NMR paper] Solution and high-pressure NMR studies of the structure, dynamics and stability of the cross-reactive allergenic cod parvalbumin Gad m 1.
Solution and high-pressure NMR studies of the structure, dynamics and stability of the cross-reactive allergenic cod parvalbumin Gad m 1.
Related Articles Solution and high-pressure NMR studies of the structure, dynamics and stability of the cross-reactive allergenic cod parvalbumin Gad m 1.
Proteins. 2014 Aug 12;
Authors: Moraes AH, Ackerbauer D, Kostadinova M, Bublin M, de Oliveira GA, Ferreira F, Almeida FC, Breiteneder H, Valente AP
Abstract
Beta-parvalbumins from different fish species have been identified as the main...
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08-15-2014 12:53 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...
A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A
A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A
22 February 2012
Publication year: 2012
Source:Biophysical Journal, Volume 102, Issue 4</br>
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Outer surface protein A (OspA) is a crucial protein in the infection of Borrelia burgdorferi causing Lyme disease. We studied conformational fluctuations of OspA with high-pressure 15N/1H two-dimensional NMR along with high-pressure fluorescence spectroscopy. We found evidence within folded, native OspA for rapid local fluctuations of the...
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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] 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...
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11-17-2010 11:15 PM
[NMR paper] High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
J Mol Biol. 1997 Oct 3;272(4):573-90
Authors: Tashiro M, Tejero R, Zimmerman DE, Celda B, Nilsson B, Montelione GT
Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size...
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08-22-2010 05:08 PM
[NMR paper] Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectr
Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectroscopy.
Biochemistry. 1996 Mar 5;35(9):2845-53
Authors: Jaishree TN, Ramakrishnan V, White SW
The solution of a primary 16S rRNA-binding ribosomal protein, S17, was investigated by two- and three-dimensional homonuclear and heteronuclear magnetic resonance...