Related ArticlesWhat's in your buffer? Solute altered millisecond motions detected by solution NMR.
Biochemistry. 2013 Sep 17;52(37):6548-58
Authors: Wong M, Khirich G, Loria JP
Abstract
To date, little work has been conducted on the relationship between solute and buffer molecules and conformational exchange motion in enzymes. This study uses solution NMR to examine the effects of phosphate, sulfate, and acetate in comparison to MES- and HEPES-buffered references on the chemical shift perturbation and millisecond, chemical, or conformational exchange motions in the enzyme ribonuclease A (RNase A), triosephosphate isomerase (TIM) and HisF. The results indicate that addition of these solutes has a small effect on (1)H and (15)N chemical shifts for RNase A and TIM but a significant effect for HisF. For RNase A and TIM, Carr-Purcell-Meiboom-Gill relaxation dispersion experiments, however, show significant solute-dependent changes in conformational exchange motions. Some residues show loss of millisecond motions relative to the reference sample upon addition of solute, whereas others experience an enhancement. Comparison of exchange parameters obtained from fits of dispersion data indicates changes in either or both equilibrium populations and chemical shifts between conformations. Furthermore, the exchange kinetics are altered in many cases. The results demonstrate that common solute molecules can alter observed enzyme millisecond motions and play a more active role than what is routinely believed.
What’s in Your Buffer? Solute Altered MillisecondMotions Detected by Solution NMR
What’s in Your Buffer? Solute Altered MillisecondMotions Detected by Solution NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi400973e/aop/images/medium/bi-2013-00973e_0013.gif
Biochemistry
DOI: 10.1021/bi400973e
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08-31-2013 06:18 AM
[NMR paper] On the use of ultracentrifugal devices for sedimented solute NMR.
On the use of ultracentrifugal devices for sedimented solute NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles On the use of ultracentrifugal devices for sedimented solute NMR.
J Biomol NMR. 2012 Oct;54(2):123-7
Authors: Bertini I, Engelke F, Gonnelli L, Knott B, Luchinat C, Osen D, Ravera E
Abstract
We have recently proposed sedimented solute NMR (SedNMR) as a solid-state method to access biomolecules without the need of crystallization or other...
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02-13-2013 12:47 PM
On the use of ultracentrifugal devices for sedimented solute NMR
On the use of ultracentrifugal devices for sedimented solute NMR
Abstract We have recently proposed sedimented solute NMR (SedNMR) as a solid-state method to access biomolecules without the need of crystallization or other sample manipulation. The drawback of SedNMR is that samples are intrinsically diluted and this is detrimental for the signal intensity. Ultracentrifugal devices can be used to increase the amount of sample inside the rotor, overcoming the intrinsic sensitivity limitation of the method. We designed two different devices and we here report the directions for using...
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08-13-2012 04:40 AM
(1)H-Detected (13)C Photo-CIDNP as a Sensitivity Enhancement Tool in Solution NMR.
(1)H-Detected (13)C Photo-CIDNP as a Sensitivity Enhancement Tool in Solution NMR.
(1)H-Detected (13)C Photo-CIDNP as a Sensitivity Enhancement Tool in Solution NMR.
J Am Chem Soc. 2011 May 6;
Authors: Lee JH, Sekhar A, Cavagnero S
NMR is a powerful yet intrinsically insensitive technique. The applicability of NMR to chemical and biological systems would be substantially extended by new approaches going beyond current signal-to-noise capabilities. Here, we exploit the large enhancements arising from (13)C photochemically induced dynamic nuclear...
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05-10-2011 05:11 PM
1H-Detected 13C Photo-CIDNP as a Sensitivity Enhancement Tool in Solution NMR
1H-Detected 13C Photo-CIDNP as a Sensitivity Enhancement Tool in Solution NMR
Jung Ho Lee, Ashok Sekhar and Silvia Cavagnero
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja111613c/aop/images/medium/ja-2010-11613c_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja111613c
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http://feeds.feedburner.com/~r/acs/jacsat/~4/nDw3hSNxR80
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05-06-2011 05:57 PM
[NMR paper] Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
Related Articles Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
J Am Chem Soc. 2005 Sep 7;127(35):12263-72
Authors: Vogel A, Katzka CP, Waldmann H, Arnold K, Brown MF, Huster D
The human N-ras protein binds to cellular membranes by insertion of two covalently bound posttranslational lipid modifications, which is crucial for its...
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12-01-2010 06:56 PM
[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...
What's in your buffer? Solute altered millisecond motions detected by solution NMR.
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