RNA structure refinement using NMR solvent accessibility data.
Sci Rep. 2017 Jul 14;7(1):5393
Authors: Hartlmüller C, Günther JC, Wolter AC, Wöhnert J, Sattler M, Madl T
Abstract
NMR spectroscopy is a powerful technique to study ribonucleic acids (RNAs) which are key players in a plethora of cellular processes. Although the NMR toolbox for structural studies of RNAs expanded during the last decades, they often remain challenging. Here, we show that solvent paramagnetic relaxation enhancements (sPRE) induced by the soluble, paramagnetic compound Gd(DTPA-BMA) provide a quantitative measure for RNA solvent accessibility and encode distance-to-surface information that correlates well with RNA structure and improves accuracy and convergence of RNA structure determination. Moreover, we show that sPRE data can be easily obtained for RNAs with any isotope labeling scheme and is advantageous regarding sample preparation, stability and recovery. sPRE data show a large dynamic range and reflect the global fold of the RNA suggesting that they are well suited to identify interaction surfaces, to score structural models and as restraints in RNA structure determination.
[NMR paper] Solvent-accessibility of discrete residue positions in the polypeptide hormone glucagon by (19)F-NMR observation of 4-fluorophenylalanine.
Solvent-accessibility of discrete residue positions in the polypeptide hormone glucagon by (19)F-NMR observation of 4-fluorophenylalanine.
Related Articles Solvent-accessibility of discrete residue positions in the polypeptide hormone glucagon by (19)F-NMR observation of 4-fluorophenylalanine.
J Biomol NMR. 2017 May 15;:
Authors: Hou Y, Hu W, Li X, Skinner JJ, Liu D, Wüthrich K
Abstract
The amino acid 4-fluoro-L-phenylalanine (4F-Phe) was introduced at the positions of Phe6 and Phe22 in the 29-residue polypeptide hormone...
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Solvent-accessibility of discrete residue positions in the polypeptide hormone glucagon by 19 F-NMR observation of 4-fluorophenylalanine
Solvent-accessibility of discrete residue positions in the polypeptide hormone glucagon by 19 F-NMR observation of 4-fluorophenylalanine
Abstract
The amino acid 4-fluoro-l-phenylalanine (4F-Phe) was introduced at the positions of Phe6 and Phe22 in the 29-residue polypeptide hormone glucagon by expressing glucagon in E. coli in the presence of an excess of 4F-Phe. Glucagon regulates blood glucose homeostasis by interaction with the glucagon receptor (GCGR), a class B GPCR. By referencing to the 4F-Phe chemical shifts at varying D2O concentrations, the...
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[NMR paper] Refinement of NMR structures using implicit solvent and advanced sampling techniques.
Refinement of NMR structures using implicit solvent and advanced sampling techniques.
Related Articles Refinement of NMR structures using implicit solvent and advanced sampling techniques.
J Am Chem Soc. 2004 Dec 15;126(49):16038-47
Authors: Chen J, Im W, Brooks CL
NMR biomolecular structure calculations exploit simulated annealing methods for conformational sampling and require a relatively high level of redundancy in the experimental restraints to determine quality three-dimensional structures. Recent advances in generalized Born (GB)...
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[NMR paper] Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
Related Articles Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
J Biol Chem. 2004 Feb 13;279(7):5699-707
Authors: Olofsson A, Ippel JH, Wijmenga SS, Lundgren E, Ohman A
The human plasma protein transthyretin (TTR) may form fibrillar protein deposits that are associated with both inherited and idiopathic amyloidosis. The present study utilizes solution nuclear magnetic resonance spectroscopy, in combination with...
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[NMR paper] Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
Related Articles Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8648-53
Authors: Ippel JH, Olofsson A, Schleucher J, Lundgren E, Wijmenga SS
Amyloid is the result of an anomalous protein and peptide aggregation, leading to the formation of insoluble fibril deposits. At present, 18 human diseases have been associated with amyloid deposits-e.g., Alzheimer's disease and Prion-transmissible...
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[NMR paper] Evaluation of Solvent Accessibility to the [Fe(4)S(4)] Binding Pocket in Native and T
Evaluation of Solvent Accessibility to the Binding Pocket in Native and Tyr19 Mutant High Potential Iron Proteins by (1)H-(15)N HMQC and (19)F NMR Experiments.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Evaluation of Solvent Accessibility to the Binding Pocket in Native and Tyr19 Mutant High Potential Iron Proteins by (1)H-(15)N HMQC and (19)F NMR Experiments.
Inorg Chem. 1996 Feb 28;35(5):1121-1125
Authors: Li D, Agarwal A, Cowan JA
The solvent accessibility of Chromatium...
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[NMR paper] Structure refinement of the glucocorticoid receptor-DNA binding domain from NMR data
Structure refinement of the glucocorticoid receptor-DNA binding domain from NMR data by relaxation matrix calculations.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure refinement of the glucocorticoid receptor-DNA binding domain from NMR data by relaxation matrix calculations.
J Mol Biol. 1995 Apr 7;247(4):689-700
Authors: van Tilborg MA, Bonvin AM, HÃ¥rd K, Davis AL, Maler B, Boelens R, Yamamoto KR, Kaptein R
The solution structure of the glucocorticoid...
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[NMR paper] A branch and bound algorithm for protein structure refinement from sparse NMR data se
A branch and bound algorithm for protein structure refinement from sparse NMR data sets.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A branch and bound algorithm for protein structure refinement from sparse NMR data sets.
J Mol Biol. 1999 Jan 29;285(4):1691-710
Authors: Standley DM, Eyrich VA, Felts AK, Friesner RA, McDermott AE
We describe new methods for predicting protein tertiary structures to low resolution given the specification of secondary structure and a...