Using a combination of high-powered computers and advanced experimental magnetic resonance data, a Florida State University biophysical chemist has developed techniques that improve the way scientists can study and predict the structure and dynamics of proteins found in the human body.
Developing NMR Methods to Analyse Large Proteins - Labmate Online
Developing NMR Methods to Analyse Large Proteins - Labmate Online
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Developing NMR Methods to Analyse Large Proteins
Labmate Online
The award will total nearly $373000 over three years to help the lab develop fast and efficient assignment methods for large proteins by NMR and make these methods accessible to the structural biology community. â??NMR spectroscopy has still a tremendous ...
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12-14-2011 07:14 PM
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins
Abstract We report enhanced sensitivity NMR measurements of intrinsically disordered proteins in the presence of paramagnetic relaxation enhancement (PRE) agents such as Ni2+-chelated DO2A. In proton-detected 1H-15N SOFAST-HMQC and carbon-detected (H-flip)13CO-15N experiments, faster longitudinal relaxation enables the usage of even shorter interscan delays. This results in higher NMR signal intensities per units of experimental time, without adverse line...
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10-21-2011 10:04 PM
Sr. Scientist / Principal Scientist ? Analytical Chemistry ? NMR | Pfizer Research and Development
Sr. Scientist / Principal Scientist ? Analytical Chemistry ? NMR | Pfizer Research and Development
US - Groton, CT, QualificationsTraining & Education:- Doctoral degree in chemistry (analytical or organic) or equivalent with 0-5years of experience in utilization of NMR in Industrial applications or masters degr
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07-22-2011 10:39 PM
[NMR paper] NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
Related Articles NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
J Am Chem Soc. 2005 Sep 14;127(36):12620-6
Authors: Torizawa T, Ono AM, Terauchi T, Kainosho M
The unambiguous assignment of the aromatic ring resonances in proteins has been severely hampered by the inherently poor sensitivities of the currently available methodologies developed for uniformly 13C/15N-labeled...
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12-01-2010 06:56 PM
[NMR paper] NMR spin relaxation methods for characterization of disorder and folding in proteins.
NMR spin relaxation methods for characterization of disorder and folding in proteins.
Related Articles NMR spin relaxation methods for characterization of disorder and folding in proteins.
J Mol Graph Model. 2001;19(1):3-12
Authors: Bracken C
The flexibility and dynamics of proteins directly influence the processes of protein folding, recognition, and function. NMR spin relaxation methods are used to assess the dynamics and mobility of proteins, for fast ps and ns motions as well as slower microsecond and ms events. The degree of protein...
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11-19-2010 08:32 PM
Scientist develops new, innovative methods for characterizing proteins - Eureka! Scie
Scientist develops new, innovative methods for characterizing proteins - Eureka! Science News
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Eureka! Science News
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Scientist develops new, innovative methods for characterizing proteins
Eureka! Science News
Nuclear magnetic resonance (NMR) data are first collected for a particular protein that is being analyzed. (NMR is a research tool that utilizes high ...
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10-20-2010 06:50 AM
Using NMR to study fast dynamics in proteins: methods and applications.
Using NMR to study fast dynamics in proteins: methods and applications.
Related Articles Using NMR to study fast dynamics in proteins: methods and applications.
Curr Opin Pharmacol. 2010 Oct 6;
Authors: Sapienza PJ, Lee AL
Proteins exist not as singular structures with precise coordinates, but rather as fluctuating bodies that move rapidly through an enormous number of conformational substates. These dynamics have important implications for understanding protein function and for structure-based drug design. NMR spectroscopy is particularly well...
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10-12-2010 02:52 PM
[NMR paper] Structural analysis of non-native states of proteins by NMR methods.
Structural analysis of non-native states of proteins by NMR methods.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural analysis of non-native states of proteins by NMR methods.
Curr Opin Struct Biol. 1996 Feb;6(1):24-30
Authors: Shortle DR
Established NMR methods are increasingly being applied to the non-native states of proteins. For small denatured proteins, full assignment of proton, 15N and 13C resonances is often straightforward. Sensitive methods exist...
Scientist develops new methods for characterising proteins
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