Related ArticlesElucidation of the protein folding landscape by NMR.
Methods Enzymol. 2005;394:299-321
Authors: Dyson HJ, Wright PE
NMR is one of the few experimental methods that can provide detailed insights into the structure and dynamics of unfolded and partly folded states of proteins. Mapping the protein folding landscape is of central importance to understanding the mechanism of protein folding. In addition, it is now recognized that many proteins are intrinsically unstructured in their functional states, while partly folded states of several cellular proteins have been implicated in amyloid disease. NMR is uniquely suited to characterize the structures present in the conformational ensemble and probe the dynamics of the polypeptide chain in unfolded and partially folded protein states.
Mapping the Landscape of RNA Dynamics with NMR Spectroscopy.
Mapping the Landscape of RNA Dynamics with NMR Spectroscopy.
Mapping the Landscape of RNA Dynamics with NMR Spectroscopy.
Acc Chem Res. 2011 Sep 6;
Authors: Rinnenthal J, Buck J, Ferner J, Wacker A, Fu?rtig B, Schwalbe H
Abstract
Among the three major classes of biomacromolecules (DNA, RNA, and proteins) RNA's pronounced dynamics are the most explicitly linked to its wide variety of functions, which include catalysis and the regulation of transcription, translation, and splicing. These functions are mediated by a range of RNA...
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09-08-2011 06:50 PM
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Sci China Life Sci. 2011 Feb;54(2):101-11
Authors: Feng W, Pan L, Zhang M
NMR spectroscopy and X-ray crystallography are two premium methods for determining the atomic structures of macro-biomolecular complexes. Each method has unique strengths and...
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02-15-2011 07:17 PM
[NMR paper] The fumarate sensor DcuS: progress in rapid protein fold elucidation by combining pro
The fumarate sensor DcuS: progress in rapid protein fold elucidation by combining protein structure prediction methods with NMR spectroscopy.
Related Articles The fumarate sensor DcuS: progress in rapid protein fold elucidation by combining protein structure prediction methods with NMR spectroscopy.
J Magn Reson. 2005 Apr;173(2):310-6
Authors: Meiler J, Baker D
We illustrate how moderate resolution protein structures can be rapidly obtained by interlinking computational prediction methodologies with un- or partially assigned NMR data. To...
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11-25-2010 08:21 PM
[NMR paper] Protein structure elucidation from minimal NMR data: the CLOUDS approach.
Protein structure elucidation from minimal NMR data: the CLOUDS approach.
Related Articles Protein structure elucidation from minimal NMR data: the CLOUDS approach.
Methods Enzymol. 2005;394:261-95
Authors: Grishaev A, Llinás M
In this chapter we review automated methods of protein NMR data analysis and expand on the assignment-independent CLOUDS approach. As presented, given a set of reliable NOEs it is feasible to derive a spatial H-atom distribution that provides a low-resolution image of the protein structure. In order to generate such a...
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11-24-2010 11:14 PM
[NMR paper] Probing the kinetic landscape of transient peptide-protein interactions by use of pep
Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin.
Related Articles Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin.
J Am Chem Soc. 2003 Oct 15;125(41):12432-42
Authors: Tolkatchev D, Xu P, Ni F
Protein-ligand interactions may lead to the formation of multiple...
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11-24-2010 09:16 PM
[NMR paper] NMR elucidation of early folding hierarchy in HIV-1 protease.
NMR elucidation of early folding hierarchy in HIV-1 protease.
Related Articles NMR elucidation of early folding hierarchy in HIV-1 protease.
J Biol Chem. 2003 May 30;278(22):19980-5
Authors: Bhavesh NS, Sinha R, Mohan PM, Hosur RV
Folding studies on proteases by the conventional hydrogen exchange experiments are severely hampered because of interference from the autolytic reaction in the interpretation of the exchange data. We report here NMR identification of the hierarchy of early conformational transitions (folding propensities) in HIV-1...
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11-24-2010 09:01 PM
[NMR paper] Protein structure elucidation from NMR proton densities.
Protein structure elucidation from NMR proton densities.
Related Articles Protein structure elucidation from NMR proton densities.
Proc Natl Acad Sci U S A. 2002 May 14;99(10):6713-8
Authors: Grishaev A, Llinas M
The NMR-generated foc proton density affords a template to which the molecule has to be fitted to derive the structure. Here we present a computational protocol that achieves this goal. H(N) atoms are readily recognizable from (1)H/(2)H exchange or (1)H/(15)N heteronuclear single quantum correlation (HSQC) experiments. The primary...
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11-24-2010 08:49 PM
[NMR paper] The pressure-temperature free energy-landscape of staphylococcal nuclease monitored b
The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.
Related Articles The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.
J Mol Biol. 2000 Apr 28;298(2):293-302
Authors: Lassalle MW, Yamada H, Akasaka K
The thermodynamic stability of staphylococcal nuclease was studied against the variation of both temperature and pressure by utilizing (1)H NMR spectroscopy at 750 MHz in 20 mM Mes buffer containing 99.9 % (2)H(2)O, pH 5.3. Equilibrium fractions of folded...
Elucidation of the protein folding landscape by NMR.
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