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The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: An Analysis of NMR J Couplings in Four Different Protein Structures.
Molecules
June 2024
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Long-range HNCO NMR spectra for proteins show crosspeaks due to J, J, J, and J couplings. The J couplings are transmitted through hydrogen bonds and their sizes are correlated to hydrogen bond lengths. We collected long-range HNCO data at a series of temperatures for four protein structures.
View Article and Find Full Text PDFPotential Energy Surfaces of HN(CH)SX:CO for X = F, Cl, NC, CN, CCH, and H: N···C Tetrel Bonds and O···S Chalcogen Bonds.
J Phys Chem A
August 2019
Instituto de Química Médica (CSIC) , Juan de la Cierva, 3 , E-28006 Madrid , Spain.
MP2/aug'-cc-pVTZ calculations have been performed in search of complexes, molecules, and transition structures on the HN(CH)SX:CO potential energy surfaces, for X = F, Cl, NC, CN, CCH, and H. Complexes stabilized by traditional N···C tetrel bonds and O···S chalcogen bonds exist on all surfaces and are bound relative to the isolated monomers. Molecules stabilized by an N-C covalent bond and an O···S chalcogen bond are found when X = F, Cl, and NC, but only the HN(CH)SF:CO molecule is bound.
View Article and Find Full Text PDFMeasurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments.
J Magn Reson
September 2009
Complex Carbohydrate Research Center, The University of Georgia, Athens, GA 30602, USA.
Residual dipolar couplings (RDCs) between NC' and NC(alpha) atoms in polypeptide backbones of proteins contain information on the orientation of bond vectors that is complementary to that contained in NH RDCs. The (1)J(NC)(alpha) and (2)J(NC)(alpha) scalar couplings between these atoms also display a Karplus relation with the backbone torsion angles and report on secondary structure. However, these N-C couplings tend to be small and they are frequently unresolvable in frequency domain spectra having the broad lines characteristic of large proteins.
View Article and Find Full Text PDFMore line narrowing in TROSY by decoupling of long-range couplings: shift correlation and 1JNC' coupling constant measurements.
J Magn Reson
October 2004
Department of Inorganic and Analytical Chemistry, University of Debrecen, Egyetem tér 1, H-4010 Debrecen, Hungary.
Since the introduction of RDCs in high-resolution NMR studies of macromolecules, there is a growing interest in the development of accurate, and sensitive methods for determining coupling constants. Most methods for extracting these couplings are based on the measurement of the splitting between multiplet components in J-coupled spectra. However, these methods are often unreliable since undesired multiple-bond couplings can considerably broaden the multiplet components and consequently make accurate determination of their position difficult.
View Article and Find Full Text PDFQuantification of H/D isotope effects on protein hydrogen-bonds by h3JNC' and 1JNC' couplings and peptide group 15N and 13C' chemical shifts.
J Biomol NMR
July 2004
Division of Structural Biology, Biozentrum der Universität Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
The effect of hydrogen/deuterium exchange on protein hydrogen bond coupling constants (h3)J(NC') has been investigated in the small globular protein ubiquitin. The couplings across deuterated or protonated hydrogen bonds were measured by a long-range quantitative HA(CACO)NCO experiment. The analysis is combined with a determination of the H(N)/D(N) isotope effect on the amide group (1)J(NC') couplings and the (15)N and (13)C' chemical shifts.
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