Related ArticlesThe hydration of proteins in solutions by self-diffusion coefficients. NMR study.
Biochim Biophys Acta. 1996 Apr 17;1289(3):312-4
Authors: Baranowska HM, Olszewski KJ
The hydration of the globular (lysozyme, albumin) and fibrillar (fibrinogen) proteins in solution has been determined from the measurements of the self-diffusion coefficient by NMR pulsed gradient method. It has been concluded that the concentration dependencies of the self-diffusion coefficient of water molecules in protein solution are controlled by two additive factors: obstruction effect correlated with the protein dimension and direct hydration effect proportional to the number of the adsorption sites on the protein surface.
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Abstract We present new NMR methods to measure slow translational diffusion coefficients of biomolecules. Like the heteronuclear stimulated echo experiment (XSTE), these new methods rely on the storage of information about spatial localization during the diffusion delay as longitudinal polarization of nuclei with long T1 such as nitrogen-15. The new BEST-XSTE sequence combines features of Band-selective Excitation Short-Transient (BEST) and XSTE methods. By...
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[NMR paper] NMR relaxation and water self-diffusion studies in whey protein solutions and gels.
NMR relaxation and water self-diffusion studies in whey protein solutions and gels.
Related Articles NMR relaxation and water self-diffusion studies in whey protein solutions and gels.
J Agric Food Chem. 2005 Aug 24;53(17):6784-90
Authors: Colsenet R, Mariette F, Cambert M
The changes in water proton transverse relaxation behavior induced by aggregation of whey proteins are explained in terms of the simple molecular processes of diffusion and chemical exchange. The water self-diffusion coefficient was measured in whey protein solutions and...
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[NMR paper] Diffusion of polyethyleneglycols in casein solutions and gels as studied by pulsed fi
Diffusion of polyethyleneglycols in casein solutions and gels as studied by pulsed field gradient NMR.
Related Articles Diffusion of polyethyleneglycols in casein solutions and gels as studied by pulsed field gradient NMR.
Magn Reson Imaging. 2005 Feb;23(2):347-8
Authors: Colsenet R, Soderman O, Mariette F
Molecular transport characterized by diffusion coefficients is a key feature of food processes and especially in dairy processes. Caseins represent 80% of the protein content in milk and are directly involved in the formation of dairy gels....
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[NMR paper] Capillary array electrophoretic NMR of proteins in biological buffer solutions.
Capillary array electrophoretic NMR of proteins in biological buffer solutions.
Related Articles Capillary array electrophoretic NMR of proteins in biological buffer solutions.
J Magn Reson. 1999 Dec;141(2):355-9
Authors: He Q, Liu Y, Sun H, Li E
The capillary array electrophoretic NMR (CA-ENMR) was developed to study protein mixtures in biological buffer solutions of high ionic strength. By enhancing the strength of the effective electric field across the sample, the technique permits the detection of the electrophoretic motion of 1 mM...
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[NMR paper] A solid-state NMR study of protein hydration and stability.
A solid-state NMR study of protein hydration and stability.
Related Articles A solid-state NMR study of protein hydration and stability.
Pharm Res. 1998 Dec;15(12):1816-21
Authors: Separovic F, Lam YH, Ke X, Chan HK
PURPOSE: The mobility of protein in powders at different hydration levels was studied in relation to aggregation and activity. METHODS: Magic angle spinning 13C, 15N, 1H, 2H, and 17O NMR techniques were used to determine changes in the mobility of surface residues in proteins as a function of hydration and related to changes in...
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[NMR paper] A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
Biophys Chem. 1997 Apr 22;65(2-3):179-87
Authors: Price WS, Nara M, Arata Y
Pulsed field gradient NMR is a convenient alternative to traditional methods for measuring diffusion of biological macromolecules. In the present study, pulsed field gradient NMR was...
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[NMR paper] A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A pulsed field gradient NMR study of the aggregation and hydration of parvalbumin.
Biophys Chem. 1997 Apr 22;65(2-3):179-87
Authors: Price WS, Nara M, Arata Y
Pulsed field gradient NMR is a convenient alternative to traditional methods for measuring diffusion of biological macromolecules. In the present study, pulsed field gradient NMR was...
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[NMR paper] NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.
NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.
Related Articles NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.
J Biomol NMR. 1992 Sep;2(5):447-65
Authors: Liepinsh E, Otting G, Wüthrich K
Hydroxyl groups of serine and threonine, and to some extent also tyrosine are usually located on or near the surface of proteins. NMR observations of the hydroxyl protons is therefore of interest to support investigations of the protein surface in solution, and knowledge of the...