Related ArticlesPractical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance.
J Magn Reson. 1999 Aug;139(2):371-6
Authors: Balazs YS, Thompson LK
Simple modifications of the rotational resonance experiment substantially reduce the total experimental time needed to measure weak homonuclear dipolar couplings, a critical factor for achieving routine internuclear distance measurements in large biomolecular systems. These modifications also address several problems cited in the literature. Here we introduce a constant-time rotational resonance experiment that eliminates the need for control spectra to correct for effects from variable RF heating, particularly critical for accurate long-distance measurements. This reduces the total number of experiments needed by as much as a factor of 2. Other improvements incorporated include achieving selective inversion with a delay rather than a weak pulse (P. R. Costa et al., J. Am. Chem. Soc. 119, 10487-10493, 1997), which we observe results in the elimination of oscillations in peak intensities for short mixing time points. This reduces the total experiment time in two ways. First, there is no longer a need to average different "zero"-time points (S. O. Smith et al., Biochemistry 33, 6334-6341, 1994) to correct for intensity variations. Second, short-mixing-time lineshape differences observed in large membrane-bound proteins only appear with the weak-pulse inversion and not when using the delay inversion. Consistent lineshapes between short and long mixing times permit the use of a single spectrum for subtraction of natural abundance background signals from all labeled-protein time points. Elimination of these effects improves the accuracy and efficiency of rotational resonance internuclear distance measurements.
Protein NMR - A Practical Guide - Solid-state MAS NMR Spectra
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Spectrum Descriptions
This page contains a list of some solid-state magic-angle spinning (MAS) NMR experiments which are useful for protein solid-state MAS NMR assignment and structure calculations. For each experiment there is short description and an illustration showing the observed magnetisation...
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11-07-2011 04:17 AM
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Abstract We present new NMR methods to measure slow translational diffusion coefficients of biomolecules. Like the heteronuclear stimulated echo experiment (XSTE), these new methods rely on the storage of information about spatial localization during the diffusion delay as longitudinal polarization of nuclei with long T1 such as nitrogen-15. The new BEST-XSTE sequence combines features of Band-selective Excitation Short-Transient (BEST) and XSTE methods. By...
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05-24-2011 10:00 AM
Solid-state NMR spectroscopy on complex biomolecules.
Solid-state NMR spectroscopy on complex biomolecules.
Solid-state NMR spectroscopy on complex biomolecules.
Angew Chem Int Ed Engl. 2010 Nov 2;49(45):8346-57
Authors: Renault M, Cukkemane A, Baldus M
Biomolecular applications of NMR spectroscopy are often merely associated with soluble molecules or magnetic resonance imaging. However, since the late 1970s, solid-state NMR (ssNMR) spectroscopy has demonstrated its ability to provide atomic-level insight into complex biomolecular systems ranging from lipid bilayers to complex biomaterials. In the...
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02-15-2011 07:17 PM
[NMR paper] Synthesis, enhanced fusogenicity, and solid state NMR measurements of cross-linked HI
Synthesis, enhanced fusogenicity, and solid state NMR measurements of cross-linked HIV-1 fusion peptides.
Related Articles Synthesis, enhanced fusogenicity, and solid state NMR measurements of cross-linked HIV-1 fusion peptides.
Biochemistry. 2003 Apr 1;42(12):3527-35
Authors: Yang R, Yang J, Weliky DP
In the HIV-1 gp41 and other viral fusion proteins, the minimal oligomerization state is believed to be trimeric with three N-terminal fusion peptides inserting into the membrane in close proximity. Previous studies have demonstrated that the...
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11-24-2010 09:01 PM
[NMR paper] Solid state NMR measurements of conformation and conformational distributions in the
Solid state NMR measurements of conformation and conformational distributions in the membrane-bound HIV-1 fusion peptide.
Related Articles Solid state NMR measurements of conformation and conformational distributions in the membrane-bound HIV-1 fusion peptide.
J Mol Graph Model. 2001;19(1):129-35
Authors: Yang J, Parkanzky PD, Khunte BA, Canlas CG, Yang R, Gabrys CM, Weliky DP
The solid state NMR lineshape of a protein backbone carbonyl nucleus is a general diagnostic of the local conformational distribution in the vicinity of that nucleus. In...
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11-19-2010 08:32 PM
[NMR paper] Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemota
Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
Biochemistry. 1997 Feb 18;36(7):1699-703
Authors: Wang J, Balazs YS, Thompson LK
The Escherichia coli serine receptor senses serine levels in the environment and transmits this information across the bacterial inner membrane to...
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08-22-2010 03:31 PM
[NMR paper] Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemota
Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
Biochemistry. 1997 Feb 18;36(7):1699-703
Authors: Wang J, Balazs YS, Thompson LK
The Escherichia coli serine receptor senses serine levels in the environment and transmits this information across the bacterial inner membrane to...
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08-22-2010 03:03 PM
[NMR paper] 31P solid-state NMR measurements used to detect interactions between NADPH and water
31P solid-state NMR measurements used to detect interactions between NADPH and water and to determine the ionisation state of NADPH in a protein-ligand complex subjected to low-level hydration.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 31P solid-state NMR measurements used to detect interactions between NADPH and water and to determine the ionisation state of NADPH in a protein-ligand complex subjected to low-level hydration.
Eur J Biochem. 1996 Jan...
Practical methods for solid-state NMR distance measurements on large biomolecules: co
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