Related ArticlesDirect identification of NH...N hydrogen bonds in non-canonical base pairs of RNA by NMR spectroscopy.
Nucleic Acids Res. 1999 Aug 1;27(15):3104-10
Authors: Wöhnert J, Dingley AJ, Stoldt M, Görlach M, Grzesiek S, Brown LR
It is shown that the recently developed quantitative J(NN)HNN-COSY experiment can be used for the direct identification of hydrogen bonds in non-canonical base pairs in RNA. Scalar(2h)J(NN)couplings across NH.N hydrogen bonds are observed in imino hydrogen bonded GA base pairs of the hpGA RNA molecule, which contains a tandem GA mismatch, and in the reverse Hoogsteen AU base pairs of the E-loop of Escherichia coli 5S rRNA. These scalar couplings correlate the imino donor(15)N nucleus of guanine or uridine with the acceptor N1 or N7 nucleus of adenine. The values of the corresponding(2h)J(NN)coupling constants are similar in size to those observed in Watson-Crick base pairs. The reverse Hoogsteen base pairs could be directly detected for the E-loop of E.coli 5S rRNA both in the free form and in a complex with the ribosomal protein L25. This supports the notion that the E-loop is a pre-folded RNA recognition site that is not subject to significant induced conformational changes. Since Watson-Crick GC and AU base pairs are also readily detected the HNN-COSY experiment provides a useful and sensitive tool for the rapid identification of RNA secondary structure elements.
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins
Abstract NOEs between the β-protons of cysteine residues across disulfide bonds in proteins provide direct information on the connectivities and conformations of these important cross-links, which are otherwise difficult to investigate. With conventional -proteins, however, fast spin diffusion processes mediated by strong dipolar interactions between geminal β-protons prohibit the quantitative measurements and thus the analyses of long-range NOEs across...
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Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
J Phys Chem B. 2011 May 2;
Authors: Hwang S, Shao Q, Williams H, Hilty C, Gao YQ
A combined simulation and experimental study was performed to investigate how methanol affects the structure of a model peptide BBA5. BBA5 forms a stable ?-hairpin-?-helix structure in aqueous solutions....
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05-04-2011 04:14 PM
[NMR paper] Ligand-induced strain in hydrogen bonds of the c-Src SH3 domain detected by NMR.
Ligand-induced strain in hydrogen bonds of the c-Src SH3 domain detected by NMR.
Related Articles Ligand-induced strain in hydrogen bonds of the c-Src SH3 domain detected by NMR.
J Mol Biol. 2000 Dec 8;304(4):497-505
Authors: Cordier F, Wang C, Grzesiek S, Nicholson LK
Changes in the molecular conformation of proteins can result from a variety of perturbations, and can play crucial roles in the regulation of biological activity. A new solution NMR method has been applied to monitor ligand-induced changes in hydrogen bond geometry in the...
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11-19-2010 08:29 PM
[NMR paper] NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by
NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy.
Related Articles NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy.
Proc Natl Acad Sci U S A. 1998 Nov 24;95(24):14147-51
Authors: Pervushin K, Ono A, Fernández C, Szyperski T, Kainosho M, Wüthrich K
This paper describes the NMR observation of 15N---15N and 1H---15N scalar couplings across the hydrogen bonds in Watson-Crick base pairs...
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11-17-2010 11:15 PM
[NMR paper] Solution NMR characterization of hydrogen bonds in a protein by indirect measurement
Solution NMR characterization of hydrogen bonds in a protein by indirect measurement of deuterium quadrupole couplings.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution NMR characterization of hydrogen bonds in a protein by indirect measurement of deuterium quadrupole couplings.
J Magn Reson. 1997 Jul;127(1):54-64
Authors: Liwang AC, Bax A
Hydrogen bonds stabilize protein and nucleic acid structure, but little direct spectroscopic data have been available for...
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08-22-2010 03:31 PM
[NMR paper] Solution NMR characterization of hydrogen bonds in a protein by indirect measurement
Solution NMR characterization of hydrogen bonds in a protein by indirect measurement of deuterium quadrupole couplings.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution NMR characterization of hydrogen bonds in a protein by indirect measurement of deuterium quadrupole couplings.
J Magn Reson. 1997 Jul;127(1):54-64
Authors: Liwang AC, Bax A
Hydrogen bonds stabilize protein and nucleic acid structure, but little direct spectroscopic data have been available for...
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08-22-2010 03:03 PM
[NMR paper] H NMR probes for inter-segmental hydrogen bonds in myoglobins.
H NMR probes for inter-segmental hydrogen bonds in myoglobins.
Related Articles H NMR probes for inter-segmental hydrogen bonds in myoglobins.
J Biochem. 1996 Jul;120(1):126-32
Authors: Yamamoto Y
NMR signals arising from the HisB5 N delta H and HisEF5 N epsilon H protons in sperm whale skeletal and horse heart myoglobins have been located for the first time in the downfield shifted portion of the spectra. The shifts and hydrogen exchange rates indicate that these His imidazole ring NH protons are involved in the inter-segmental hydrogen bonds...
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[NMR paper] Transient hydrogen bonds identified on the surface of the NMR solution structure of H
Transient hydrogen bonds identified on the surface of the NMR solution structure of Hirudin.
Related Articles Transient hydrogen bonds identified on the surface of the NMR solution structure of Hirudin.
Biochemistry. 1994 Aug 9;33(31):9303-10
Authors: Szyperski T, Antuch W, Schick M, Betz A, Stone SR, Wüthrich K
Recombinant desulfatohirudin retains largely the thrombin-inhibitory activity of natural hirudin from Hirudo medicinalis and causes at most minimal immune response in humans. With regard to potential pharmaceutical applications it is...