The samples are dissolved in solvents which contain no hydrogen atoms ...
25/04/2014 10:27:29 PM GMT
The samples are dissolved in solvents which contain no hydrogen atoms ... More...
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[NMR paper] Use of H/D isotope effects to gather information about hydrogen bonding and hydrogen exchange rates
Use of H/D isotope effects to gather information about hydrogen bonding and hydrogen exchange rates
Publication date: Available online 11 October 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Mitsuhiro Takeda , Yohei Miyanoiri , Tsutomu Terauchi , Chin-Jiun Yang , Masatsune Kainosho</br>
Polar side-chains in proteins play important roles in formingand maintaining three-dimensional structures, and thus participate invarious biological functions. Until recently, most protein NMR studieshave focused onthe non-exchangeable protons of amino acid...
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10-11-2013 10:43 AM
[U. of Ottawa NMR Facility Blog] Protic Samples in Aprotic Solvents
Protic Samples in Aprotic Solvents
The appearance of the 1H NMR signals of protic samples in aprotic solvents depends critically on the concentration of the sample. The -OH, -NH2 or -COOH signals can have chemical shift values and line widths over a wide range due to varying extents of hydrogen bonding and chemical exchange. The concentration can also determine whether or not one is able to observe J coupling between and -OH proton and other protons in the sample. An example of this is illustrated below. The figure shows the spectrum of methanol in deuterated acetone. The spectrum on the...
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03-17-2012 07:32 AM
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
Abstract Comprehensive application of solution NMR spectroscopy to studies of macromolecules remains fundamentally limited by the molecular rotational correlation time. For proteins, molecules larger than 30 kDa require complex experimental methods, such as TROSY in conjunction with isotopic labeling schemes that are often expensive and generally reduce the potential information available. We have developed the reverse micelle encapsulation strategy as an alternative approach. Encapsulation of...
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07-15-2011 09:10 PM
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
J Biomol NMR. 2011 Jul 12;
Authors: Nucci NV, Marques BS, Bédard S, Dogan J, Gledhill JM, Moorman VR, Peterson RW, Valentine KG, Wand AL, Wand AJ
Comprehensive application of solution NMR spectroscopy to studies of macromolecules remains fundamentally limited by the molecular rotational correlation time. For proteins, molecules larger than 30*kDa require complex...
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07-13-2011 06:42 PM
[NMR paper] Elucidation of the structures of residual and dissolved pine kraft lignins using an H
Elucidation of the structures of residual and dissolved pine kraft lignins using an HMQC NMR technique.
Related Articles Elucidation of the structures of residual and dissolved pine kraft lignins using an HMQC NMR technique.
J Agric Food Chem. 2003 Oct 8;51(21):6116-27
Authors: Balakshin MY, Capanema EA, Chen CL, Gracz HS
Comparative studies on the structures of residual and dissolved lignins isolated from pine kraft pulp and pulping liquor have been undertaken using the (1)H-(13)C HMQC NMR technique, GPC, and sugar analysis to elucidate the...
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11-24-2010 09:16 PM
[NMR paper] High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.
High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.
Related Articles High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.
Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15299-302
Authors: Wand AJ, Ehrhardt MR, Flynn PF
The majority of known proteins are too large to be comprehensively examined by solution NMR methods, primarily because they tumble too slowly in solution. Here we introduce an approach to making the NMR relaxation properties of large proteins amenable to modern solution NMR...
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11-17-2010 11:15 PM
[NMR paper] Structure of lysozyme dissolved in neat organic solvents as assessed by NMR and CD sp
Structure of lysozyme dissolved in neat organic solvents as assessed by NMR and CD spectroscopies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Structure of lysozyme dissolved in neat organic solvents as assessed by NMR and CD spectroscopies.
Biotechnol Bioeng. 1999 Apr 20;63(2):242-8
Authors: Knubovets T, Osterhout JJ, Klibanov AM
The structure of the model protein hen egg-white lysozyme dissolved in water and in five neat organic...