Related ArticlesNMR triple-quantum filtered relaxation analysis of 17O-water in insulin solutions: an insight into the aggregation of insulin and the properties of its bound water.
Biophys Chem. 1998 Mar 9;70(3):231-9
Authors: Torres AM, Grieve SM, Kuchel PW
Transverse triple-quantum filtered NMR spectroscopy (TTQF) of 17O-water was used to study the properties of water in insulin solutions at different Zn2+ concentrations and pH values. It was established that strongly bound water molecules are already present in Zn-free insulin. On the assumption that the effective correlation time of a strongly bound water molecule, tau sb, is 10 ns, the apparent number of strongly bound water molecules was approximately 3 to 4 per insulin monomer. Addition of Zn2+ equivalent to approximately 2 g-atoms per hexamer did not produce substantial increases in the overall 17O-water TTQF signal intensity and apparent fraction of bound water. The dramatic enhancement of the TTQF signals observed for samples with a Zn2+/hexamer ratio greater than approximately 2:1 could be attributed to the increase in correlation time of the strongly bound water, due to the formation of higher-order oligomers of the protein.
Multiplet-filtered and gradient-selected zero-quantum TROSY experiments for 13C1H3 methyl groups in proteins
Multiplet-filtered and gradient-selected zero-quantum TROSY experiments for 13C1H3 methyl groups in proteins
Abstract Multiplet-filtered and gradient-selected heteronuclear zero-quantum coherence (gsHZQC) TROSY experiments are described for measuring 1Hâ??13C correlations for 13CH3 methyl groups in proteins. These experiments provide improved suppression of undesirable, broad outer components of the heteronuclear zero-quantum multiplet in medium-sized proteins, or in flexible sites of larger proteins, compared to previously described HZQC sequences (Tugarinov et al. in J Am Chem Soc...
nmrlearner
Journal club
0
09-17-2011 10:20 AM
[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...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] Multiple quantum filtered NMR studies of the interaction between collagen and water i
Multiple quantum filtered NMR studies of the interaction between collagen and water in the tendon.
Related Articles Multiple quantum filtered NMR studies of the interaction between collagen and water in the tendon.
J Am Chem Soc. 2002 Mar 27;124(12):3125-32
Authors: Eliav U, Navon G
We studied the physical processes and the chemical reactions involved in magnetization transfer between water and large proteins, such as collagen, in bovine Achilles tendon. Since the NMR spectrum for such proteins is broadened by very large dipolar interactions,...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF bind
NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF binding protein-5 (IGFBP-5) determined free in solution and in complex with IGF-II.
Related Articles NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF binding protein-5 (IGFBP-5) determined free in solution and in complex with IGF-II.
Eur J Biochem. 2001 Feb;268(4):1058-65
Authors: Renner C, Holak T
15N NMR relaxation rates of mini-IGFBP-5, an N-terminal insulin-like growth factor binding domain of the insulin-like growth factor...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
Water-Proton-Spin-Lattice-Relaxation Dispersion of Paramagnetic Protein Solutions
Water-Proton-Spin-Lattice-Relaxation Dispersion of Paramagnetic Protein Solutions
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 10 November 2010</br>
Galina, Diakova , Yanina, Goddard , Jean-Pierre, Korb , Robert G., Bryant</br>
The paramagnetic contributions to water proton spin-lattice relaxation rate constants in protein systems spin-labeled with nitroxide radicals were re-examined. As noted by others, the strength of the dipolar coupling between water protons and the protein-bound nitroxide radical often appears to...
nmrlearner
Journal club
0
11-11-2010 04:33 PM
[NMR paper] Strong and weak binding of water to proteins studied by NMR triple-quantum filtered r
Strong and weak binding of water to proteins studied by NMR triple-quantum filtered relaxation spectroscopy of (17)O-water.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Strong and weak binding of water to proteins studied by NMR triple-quantum filtered relaxation spectroscopy of (17)O-water.
Biophys Chem. 1997 Sep 1;67(1-3):187-98
Authors: Torres AM, Grieve SM, Chapman BE, Kuchel PW
The triple-quantum filtered (TQF) spin-echo signal of (17)O-water, in the presence...
nmrlearner
Journal club
0
08-22-2010 05:08 PM
[NMR paper] Observation of reorientationally hindered water in biological tissue using triple qua
Observation of reorientationally hindered water in biological tissue using triple quantum filtered 17O-NMR.
Related Articles Observation of reorientationally hindered water in biological tissue using triple quantum filtered 17O-NMR.
Biochim Biophys Acta. 1995 Jun 9;1244(2-3):253-8
Authors: Flesche CW, Gruwel ML, Deussen A, Schrader J
Water dynamics in aqueous biopolymer solutions often display a two-phase character, resembling water-water and water-protein interactions. Rotationally hindered water molecules in crowded protein environments...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] Characterisation by triple-quantum filtered 17O-NMR of water molecules buried in lyso
Characterisation by triple-quantum filtered 17O-NMR of water molecules buried in lysozyme and trapped in a lysozyme-inhibitor complex.
Related Articles Characterisation by triple-quantum filtered 17O-NMR of water molecules buried in lysozyme and trapped in a lysozyme-inhibitor complex.
Biophys Chem. 1999 Mar 29;77(2-3):111-21
Authors: Baguet E, Hennebert N
Triple-quantum filtering NMR sequences were used to study the multiexponential relaxation behaviour of H2 17O in the presence of hen egg white lysozyme. By this means, the fraction and the...
NMR triple-quantum filtered relaxation analysis of 17O-water in insulin solutions: an
Linear Mode
