Related ArticlesWater behavior in bacterial spores by deuterium NMR spectroscopy.
J Phys Chem B. 2014 Jul 31;118(30):8945-55
Authors: Friedline AW, Zachariah MM, Johnson K, Thomas KJ, Middaugh AN, Garimella R, Powell DR, Vaishampayan PA, Rice CV
Abstract
Dormant bacterial spores are able to survive long periods of time without nutrients, withstand harsh environmental conditions, and germinate into metabolically active bacteria when conditions are favorable. Numerous factors influence this hardiness, including the spore structure and the presence of compounds to protect DNA from damage. It is known that the water content of the spore core plays a role in resistance to degradation, but the exact state of water inside the core is a subject of discussion. Two main theories present themselves: either the water in the spore core is mostly immobile and the core and its components are in a glassy state, or the core is a gel with mobile water around components which themselves have limited mobility. Using deuterium solid-state NMR experiments, we examine the nature of the water in the spore core. Our data show the presence of unbound water, bound water, and deuterated biomolecules that also contain labile deuterons. Deuterium-hydrogen exchange experiments show that most of these deuterons are inaccessible by external water. We believe that these unreachable deuterons are in a chemical bonding state that prevents exchange. Variable-temperature NMR results suggest that the spore core is more rigid than would be expected for a gel-like state. However, our rigid core interpretation may only apply to dried spores whereas a gel core may exist in aqueous suspension. Nonetheless, the gel core, if present, is inaccessible to external water.
[NMR paper] The role of water in protein's behavior: The two dynamical crossovers studied by NMR and FTIR techniques.
The role of water in protein's behavior: The two dynamical crossovers studied by NMR and FTIR techniques.
Related Articles The role of water in protein's behavior: The two dynamical crossovers studied by NMR and FTIR techniques.
Comput Struct Biotechnol J. 2015;13:33-7
Authors: Mallamace F, Corsaro C, Mallamace D, Vasi S, Vasi C, Dugo G
Abstract
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The role of water in proteins behavior: The two dynamical crossovers studied by NMR and FTIR techniques
The role of water in proteins behavior: The two dynamical crossovers studied by NMR and FTIR techniques
Publication date: Available online 15 November 2014
Source:Computational and Structural Biotechnology Journal</br>
Author(s): Francesco Mallamace , Carmelo Corsaro , Domenico Mallamace , Sebastiano Vasi , Cirino Vasi , Giacomo Dugo</br>
The role the solvent plays in determining the biological activity of proteins is of primary importance. Water is the solvent of life and proteins need at least a water monolayer covering their surface in order to become...
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[NMR paper] Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.
Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.
Related Articles Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.
Biochim Biophys Acta. 2014 Jun 16;
Authors: Kinnun JJ, Mallikarjunaiah KJ, Petrache HI, Brown MF
Abstract
This article reviews the application of solid-state (2)H nuclear magnetic resonance (NMR) spectroscopy for investigating the deformation of lipid bilayers at the atomistic level. For...
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[NMR paper] Real-Time Monitoring of New Delhi Metallo-?-Lactamase Activity in Living Bacterial Cells by (1) H NMR Spectroscopy.
Real-Time Monitoring of New Delhi Metallo-?-Lactamase Activity in Living Bacterial Cells by (1) H NMR Spectroscopy.
Related Articles Real-Time Monitoring of New Delhi Metallo-?-Lactamase Activity in Living Bacterial Cells by (1) H NMR Spectroscopy.
Angew Chem Int Ed Engl. 2014 Jan 23;
Authors: Ma J, McLeod S, Maccormack K, Sriram S, Gao N, Breeze AL, Hu J
Abstract
Disconnections between in vitro responses and those observed in whole cells confound many attempts to design drugs in areas of serious medical need. A method based on 1D (1) H...
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[NMR paper] Bacterial expression and purification of the amyloidogenic peptide PAPf39 for multidimensional NMR spectroscopy.
Bacterial expression and purification of the amyloidogenic peptide PAPf39 for multidimensional NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Bacterial expression and purification of the amyloidogenic peptide PAPf39 for multidimensional NMR spectroscopy.
Protein Expr Purif. 2013 Apr;88(2):196-200
Authors: Shanmuganathan A, Bishop AC, French KC, McCallum SA, Makhatadze GI
Abstract
PAPf39 is a 39 residue peptide fragment from human...
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[NMR paper] The Heterogeneous Structural Behavior of E7 from HPV16 Revealed by NMR Spectroscopy.
The Heterogeneous Structural Behavior of E7 from HPV16 Revealed by NMR Spectroscopy.
The Heterogeneous Structural Behavior of E7 from HPV16 Revealed by NMR Spectroscopy.
Chembiochem. 2013 Aug 12;
Authors: Calçada EO, Felli IC, Hoek T, Pierattelli R
Abstract
The E7 protein from human papillomavirus (HPV) plays a key role in oncogenesis; for this reason, it is a target of great biomedical interest. To date, no high resolution information is available for the full protein. We present here the NMR characterization of the entire E7 from...
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Investigation of the dynamical properties of water in elastin by deuterium Double Qua
Investigation of the dynamical properties of water in elastin by deuterium Double Quantum Filtered NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Investigation of the dynamical properties of water in elastin by deuterium Double Quantum Filtered NMR.
J Magn Reson. 2010 Jul;205(1):86-92
Authors: Sun C, Boutis GS
The anisotropic motion of tightly bound waters of hydration in bovine nuchal ligament elastin has been studied by deuterium Double Quantum Filtered (DQF) NMR....
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[NMR paper] Quantitative evaluation of water content in a solid protein by deuterium NMR.
Quantitative evaluation of water content in a solid protein by deuterium NMR.
Related Articles Quantitative evaluation of water content in a solid protein by deuterium NMR.
Biochim Biophys Acta. 1992 Feb 26;1119(2):178-84
Authors: Tamura A, Akasaka K
A method for evaluating absolute water content in a solid protein based on deuterium NMR measurements in solution is described. By dissolving the hydrated solid protein, which has been specifically deuterium-labeled, into deuterium-depleted water and by comparing the deuterium NMR signal intensity...