Related ArticlesNMR studies of protein hydration and TEMPOL accessibility.
J Mol Biol. 2003 Sep 12;332(2):437-47
Authors: Niccolai N, Spiga O, Bernini A, Scarselli M, Ciutti A, Fiaschi I, Chiellini S, Molinari H, Temussi PA
Understanding the mechanisms of the interaction between a protein surface and its outer molecular environment is of primary relevance for the rational design of new drugs and engineered proteins. Protein surface accessibility is emerging as a new dimension of Structural Biology, since NMR methods have been developed to follow how molecules, even those different from physiological ligands, preferentially approach specific regions of the protein surface. Hen egg-white lysozyme, a paradigmatic example of the state of the art of protein structure and dynamics, has been selected as a model system to study protein surface accessibility. Bound water and soluble spin-labels have been used to investigate the interaction of this enzyme, both free and bound to the inhibitor (NAG)(3), with its molecular environment. No tightly bound water molecules were found inside the enzyme active site, which, conversely, appeared as the most exposed to visits from the soluble paramagnetic probe TEMPOL. From the presented set of data, an integrated view of lysozyme surface accessibility towards water and TEMPOL molecules is obtained.
Hydration studies on the archaeal protein Sso7d using NMR measurements and MD ... - 7thSpace Interactive (press release)
Hydration studies on the archaeal protein Sso7d using NMR measurements and MD ... - 7thSpace Interactive (press release)
<img alt="" height="1" width="1" />
Hydration studies on the archaeal protein Sso7d using NMR measurements and MD ...
7thSpace Interactive (press release)
... the hydration of the archaeal multifunctional protein Sso7d from Solfolobus solfataricus was investigated using a combination of computational and experimental data derived from molecular dynamics simulations and ePHOGSY NMR spectroscopy. ...
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10-21-2011 10:04 PM
[NMR paper] NMR spin-echo studies of hydration properties of the molecular chaperone alpha-crysta
NMR spin-echo studies of hydration properties of the molecular chaperone alpha-crystallin in the bovine lens.
Related Articles NMR spin-echo studies of hydration properties of the molecular chaperone alpha-crystallin in the bovine lens.
Biochim Biophys Acta. 2002 Jul 29;1598(1-2):46-54
Authors: Babizhayev MA, Nikolayev GN, Goryachev SN, Bours J
The water-binding properties of bovine lens alpha-crystallin, collagen from calf skin and bovine serum albumin (BSA), were investigated with various techniques. The water absorptive capacity was...
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11-24-2010 08:58 PM
[NMR paper] NMR studies of protein surface accessibility.
NMR studies of protein surface accessibility.
Related Articles NMR studies of protein surface accessibility.
J Biol Chem. 2001 Nov 9;276(45):42455-61
Authors: Niccolai N, Ciutti A, Spiga O, Scarselli M, Bernini A, Bracci L, Di Maro D, Dalvit C, Molinari H, Esposito G, Temussi PA
Characterization of protein surface accessibility represents a new frontier of structural biology. A surface accessibility investigation for two structurally well-defined proteins, tendamistat and bovine pancreatic trypsin inhibitor, is performed here by a combined...
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11-19-2010 08:44 PM
[NMR paper] NMR and molecular dynamics studies of the hydration of a zinc finger-DNA complex.
NMR and molecular dynamics studies of the hydration of a zinc finger-DNA complex.
Related Articles NMR and molecular dynamics studies of the hydration of a zinc finger-DNA complex.
J Mol Biol. 2000 Oct 6;302(5):1101-17
Authors: Tsui V, Radhakrishnan I, Wright PE, Case DA
The hydration of a high-affinity protein-DNA complex involving the three amino terminal zinc finger domains of transcription factor IIIA (TFIIIA) and a 15-base-pair DNA duplex was investigated by NMR spectroscopy and molecular dynamics (MD) simulations. Intermolecular nuclear...
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11-19-2010 08:29 PM
[NMR paper] FTIR and NMR studies on the hydration of a high-M(r) subunit of glutenin.
FTIR and NMR studies on the hydration of a high-M(r) subunit of glutenin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles FTIR and NMR studies on the hydration of a high-M(r) subunit of glutenin.
Int J Biol Macromol. 1995 Apr;17(2):74-80
Authors: Belton PS, Colquhoun IJ, Grant A, Wellner N, Field JM, Shewry PR, Tatham AS
The hydration behaviour of a purified high-M(r) subunit of glutenin has been studied using Fourier transform infra-red (FTIR) and nuclear magnetic...
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08-22-2010 03:41 AM
[NMR paper] NMR studies of protein hydration.
NMR studies of protein hydration.
Related Articles NMR studies of protein hydration.
Prog Biophys Mol Biol. 1994;61(1):61-79
Authors: Belton PS
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[NMR paper] NMR studies of protein hydration.
NMR studies of protein hydration.
Related Articles NMR studies of protein hydration.
Prog Biophys Mol Biol. 1994;61(1):61-79
Authors: Belton PS
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[NMR paper] Structural effects of hydration: studies of lysozyme by 13C solids NMR.
Structural effects of hydration: studies of lysozyme by 13C solids NMR.
Related Articles Structural effects of hydration: studies of lysozyme by 13C solids NMR.
Biopolymers. 1990 Dec;29(14):1801-6
Authors: Kennedy SD, Bryant RG
13C-nmr spectra of lysozyme obtained at 50.3 MHz using both static and magic-angle-spinning-cross-polarization methods are reported at several water contents. The line widths and consequent resolution in the hydrated material is substantially improved over that in the lyophilized protein. The line narrowing is not...
NMR studies of protein hydration and TEMPOL accessibility.
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