Related ArticlesCharacterisation 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 correlation time of water were determined in slow motion, as well as the relaxation time of water in the extreme narrowing limit. The small number of water molecules in slow motion, which is between four and five per lysozyme, seems to correspond to the 'integral' water, buried or in the cleft inside the protein, whereas water in fast motion corresponds to all other water molecules, interacting or not with the macromolecules. The same experiment was performed after addition of the inhibitor tri-N-acetylglucosamine (NAG)3. For solutions of sufficient viscosity, there were approximately three supplementary water molecules in slow motion per lysozyme, probably trapped between the protein and the inhibitor. The correlation time of these water molecules was estimated at 2 ns, which should correspond to their residence time in the complex.
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...
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[NMR paper] Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain o
Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR.
Related Articles Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR.
J Biomol NMR. 2005 Apr;31(4):295-310
Authors: Chevelkov V, Faelber K, Diehl A, Heinemann U, Oschkinat H, Reif B
Water molecules are a major determinant of protein stability and are important for understanding protein-protein interactions. We present two experiments which allow to...
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[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,...
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[NMR paper] Water molecules in DNA recognition I: hydration lifetimes of trp operator DNA in solu
Water molecules in DNA recognition I: hydration lifetimes of trp operator DNA in solution measured by NMR spectroscopy.
Related Articles Water molecules in DNA recognition I: hydration lifetimes of trp operator DNA in solution measured by NMR spectroscopy.
J Mol Biol. 1998 Oct 2;282(4):847-58
Authors: Sunnerhagen M, Denisov VP, Venu K, Bonvin AM, Carey J, Halle B, Otting G
The present NMR study investigates the residence times of the hydration water molecules associated with uncomplexed trp operator DNA in solution by measuring intermolecular...
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[NMR paper] NMR triple-quantum filtered relaxation analysis of 17O-water in insulin solutions: an
NMR 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.
Related Articles NMR 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...
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[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...
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[NMR paper] Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by
Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy.
Biochemistry. 1996 Oct 1;35(39):12694-704
Authors: Wang YX, Freedberg DI, Grzesiek S, Torchia DA, Wingfield PT, Kaufman JD, Stahl SJ, Chang CH, Hodge CN
A tetrahedrally hydrogen-bonded structural water molecule, water 301, is seen in...
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[NMR paper] Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
Related Articles Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
J Biomol NMR. 1995 Jun;5(4):415-9
Authors: Cistola DP, Hall KB
A simple approach for detecting internal water molecules in proteins in solution is described. This approach combines 19F-detected heteronuclear Overhauser and exchange spectroscopy (HOESY) with site-specific 19F substitution. The model system employed was intestinal fatty acid-binding protein complexed with...