High sensitivity and resolution solid-state NMR methods are reported, that straightforwardly select hydrogen-bonded ^(15)N-^(17)O pairs from amongst all other nitrogen and oxygen sites in peptides, to aid protein secondary and tertiary structure determination. Significantly improved sensitivity is obtained with indirect ¹H detection under fast MAS and stronger relayed dipole couplings.
[NMR paper] MAS NMR detection of hydrogen bonds for protein secondary structure characterization.
MAS NMR detection of hydrogen bonds for protein secondary structure characterization.
Related Articles MAS NMR detection of hydrogen bonds for protein secondary structure characterization.
J Biomol NMR. 2020 Mar 17;:
Authors: Friedrich D, Perodeau J, Nieuwkoop AJ, Oschkinat H
Abstract
Hydrogen bonds are essential for protein structure and function, making experimental access to long-range interactions between amide protons and heteroatoms invaluable. Here we show that measuring distance restraints involving backbone hydrogen...
nmrlearner
Journal club
0
03-19-2020 06:10 PM
MAS NMR detection of hydrogen bonds for protein secondary structure characterization
MAS NMR detection of hydrogen bonds for protein secondary structure characterization
Abstract
Hydrogen bonds are essential for protein structure and function, making experimental access to long-range interactions between amide protons and heteroatoms invaluable. Here we show that measuring distance restraints involving backbone hydrogen atoms and carbonyl- or α-carbons enables the identification of secondary structure elements based on hydrogen bonds, provides long-range contacts and validates spectral assignments. To this end, we apply specifically...
nmrlearner
Journal club
0
03-18-2020 10:42 AM
[NMR paper] Characterization of doubly ionic hydrogen bonds in protic ionic liquids by NMR deuteron quadrupole coupling constants - Differences to H-bonds in amides, peptides and proteins.
Characterization of doubly ionic hydrogen bonds in protic ionic liquids by NMR deuteron quadrupole coupling constants - Differences to H-bonds in amides, peptides and proteins.
Related Articles Characterization of doubly ionic hydrogen bonds in protic ionic liquids by NMR deuteron quadrupole coupling constants - Differences to H-bonds in amides, peptides and proteins.
Angew Chem Int Ed Engl. 2017 Sep 17;:
Authors: Ludwig R, Khudozhitkov AE, Stange P, Golub B, Paschek D, Stepanov AG, Kolokolov DI
Abstract
We present the first...
nmrlearner
Journal club
0
09-19-2017 04:40 PM
[NMR paper] Characterization of doubly ionic hydrogen bonds in protic ionic liquids by NMR deuteron quadrupole coupling constants - Differences to H-bonds in amides, peptides and proteins
Characterization of doubly ionic hydrogen bonds in protic ionic liquids by NMR deuteron quadrupole coupling constants - Differences to H-bonds in amides, peptides and proteins
We present the first deuteron quadrupole coupling constants (DQCC) for selected protic ionic liquids (PILs) measured by solid-state NMR spectroscopy. The experimental data are supported by dispersion-corrected density functional theory (DFT-D3) calculations and molecular dynamics (MD) simulations. The DQCCs of the N-D bond in the triethylammonium cations are the lowest reported for deuterons in PILs indicating...
nmrlearner
Journal club
0
09-18-2017 10:41 AM
Direct 13 C-detected NMR experiments for mapping and characterization of hydrogen bonds in RNA
Direct 13 C-detected NMR experiments for mapping and characterization of hydrogen bonds in RNA
Abstract
In RNA secondary structure determination, it is essential to determine whether a nucleotide is base-paired and not. Base-pairing of nucleotides is mediated by hydrogen bonds. The NMR characterization of hydrogen bonds relies on experiments correlating the NMR resonances of exchangeable protons and can be best performed for structured parts of the RNA, where labile hydrogen atoms are protected from solvent exchange. Functionally important regions in...
nmrlearner
Journal club
0
02-06-2016 03:10 PM
[NMR paper] Solid-state NMR investigation of the buried X-proline peptide bonds of bacteriorhodop
Solid-state NMR investigation of the buried X-proline peptide bonds of bacteriorhodopsin.
Related Articles Solid-state NMR investigation of the buried X-proline peptide bonds of bacteriorhodopsin.
Biochemistry. 2003 Apr 1;42(12):3586-93
Authors: Lansing JC, Hu JG, Belenky M, Griffin RG, Herzfeld J
The role of proline residues in the photocycle of bacteriorhodopsin (bR) is addressed using solid-state NMR. (13)C and (15)N chemical shifts from X-Pro peptide bonds in bR are assigned from REDOR difference spectra of pairwise labeled samples, and...
nmrlearner
Journal club
0
11-24-2010 09:01 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...
nmrlearner
Journal club
0
11-19-2010 08:29 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...
Characterization of peptide O?HN hydrogen bonds via1H-detected 15N/17O solid-state NMR spectroscopy
Linear Mode
