NMR paper Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic,

		BioNMR > Educational resources > Journal club
[NMR paper] Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic,

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

08-21-2010, 11:16 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,775

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic,

Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic, hydrophobic, and electrostatic interactions.

Related Articles Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic, hydrophobic, and electrostatic interactions.

Adv Exp Med Biol. 1991;302:541-60

Authors: Kumosinski TF, Pessen H, Farrell HM

The importance of water interactions with proteins in food systems is well documented. A controversy exists, however, as to the nature of these interactions and the effect of protein structural changes on them. To clarify these questions, a method has been developed for determining hydration from the protein concentration-dependence of deuteron resonance relaxation rates. Measurements were made in D2O on beta-lactoglobulin A to study effects of hydrophilic interactions, and on both casein micelles and submicelles to study hydrophobic and electrostatic effects. From the protein concentration-dependent relaxation rates, the second viral coefficients of the proteins were obtained by nonlinear regression analysis. Using either an isotropic tumbling or an intermediate asymmetry model, hydrations, upsilon, and correlation times, tau c, were calculated for the protein-associated water; from tau c, the Stokes radius, R, was obtained. Variations in upsilon and R were in accord with known structural changes in molecular states of the proteins. The NMR results are compared with hydrations and structural information derived independently from small-angle X-ray scattering.

PMID: 1746349 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR thesis] NMR Studies of Protein-DNA Interactions : Determinations of DNA Structures Recognized by Bin Recombinase and Studies of Their Roles in Protein Binding Interactions NMR Studies of Protein-DNA Interactions : Determinations of DNA Structures Recognized by Bin Recombinase and Studies of Their Roles in Protein Binding Interactions Sun, Yun (1992) NMR Studies of Protein-DNA Interactions : Determinations of DNA Structures Recognized by Bin Recombinase and Studies of Their Roles in Protein Binding Interactions. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechTHESIS:09132011-160134197 More...	nmrlearner	NMR theses	0	09-16-2011 10:02 PM
Site-resolved measurement of water-protein interactions by solution NMR. Site-resolved measurement of water-protein interactions by solution NMR. Site-resolved measurement of water-protein interactions by solution NMR. Nat Struct Mol Biol. 2011 Jan 2; Authors: Nucci NV, Pometun MS, Wand AJ The interactions of biological macromolecules with water are fundamental to their structure, dynamics and function. Historically, characterization of the location and residence times of hydration waters of proteins in solution has been quite difficult. Confining proteins within the nanoscale interior of a reverse micelle slows water...	nmrlearner	Journal club	0	01-05-2011 09:51 PM
[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] Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy. Related Articles Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy. J Am Chem Soc. 2003 Nov 5;125(44):13336-7 Authors: Lesage A, Böckmann A Using solid-state NMR carbon-proton dipolar correlation spectroscopy, we observed hydrogen exchange on the millisecond time scale between water molecules and protein protons in a solid sample. These interactions are shown to be related to important structural...	nmrlearner	Journal club	0	11-24-2010 09:16 PM
[NMR paper] Relaxation of water protons in highly concentrated aqueous protein systems studied by Relaxation of water protons in highly concentrated aqueous protein systems studied by 1H NMR spectroscopy. Related Articles Relaxation of water protons in highly concentrated aqueous protein systems studied by 1H NMR spectroscopy. Z Naturforsch C. 2001 Nov-Dec;56(11-12):1075-81 Authors: Szuminska K, Gutsze A, Kowalczyk A Concentrated Aqueous Protein Systems, Proton Relaxation Times, Slow Chemical Exchange In this paper we present proton spin-lattice (T1) and spin-spin (T2) relaxation times measured vs. concentration, temperature, pulse...	nmrlearner	Journal club	0	11-19-2010 08:44 PM
[NMR paper] Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NM Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study. Related Articles Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study. Protein Sci. 2000 Aug;9(8):1540-7 Authors: Kutyshenko VP, Cortijo M We have used the homonuclear Overhauser effect (NOE) to characterize a model protein: carbonic anhydrase B. We have obtained NOE difference spectra for this protein, centering the on-resonance signals either at the methyl-proton or at the...	nmrlearner	Journal club	0	11-19-2010 08:29 PM
[NMR paper] Effect of thermal denaturation on water-collagen interactions: NMR relaxation and dif Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis. Related Articles Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis. Biopolymers. 1999 Dec;50(7):690-6 Authors: Rochdi A, Foucat L, Renou JP The dependence of the proton spin-lattice relaxation rate, and of the enthalpy and temperature of denaturation on water content, were studied by nmr and differential scanning calorimetry (DSC) in native and...	nmrlearner	Journal club	0	11-18-2010 08:31 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

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off