NMR isotope shifts occur due to small differences in nuclear shielding when nearby atoms are different isotopes. For molecules dissolved in 1:1 H(2)O:D(2)O, the resulting mixture of N-H and N-D isotopes leads to a small splitting of resonances from adjacent nuclei. We used multidimensional NMR to measure isotope shifts for the proteins CUS-3iD and CspA. We observed four-bond ??N(ND) isotope shifts in high-resolution 2D ^(15)N-TROSY experiments of the perdeuterated proteins that correlate with...
NMR detection and conformational dependence of two, three, and four-bond isotope shifts due to deuteration of backbone amides
NMR detection and conformational dependence of two, three, and four-bond isotope shifts due to deuteration of backbone amides
Abstract
NMR isotope shifts occur due to small differences in nuclear shielding when nearby atoms are different isotopes. For molecules dissolved in 1:1 H2O:D2O, the resulting mixture of N-H and N-D isotopes leads to a small splitting of resonances from adjacent nuclei. We used multidimensional NMR to measure isotope shifts for the proteins CUS-3iD and CspA. We observed four-bond 4â??N(ND) isotope shifts in high-resolution 2D...
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04-25-2023 01:59 PM
[NMR paper] Deuteration for High-Resolution Detection of Protons in Protein Magic Angle Spinning (MAS) Solid-State NMR
Deuteration for High-Resolution Detection of Protons in Protein Magic Angle Spinning (MAS) Solid-State NMR
Proton detection developed in the last 20 years as the method of choice to study biomolecules in the solid state. In perdeuterated proteins, proton dipolar interactions are strongly attenuated, which allows yielding of high-resolution proton spectra. Perdeuteration and backsubstitution of exchangeable protons is essential if samples are rotated with MAS rotation frequencies below 60 kHz. Protonated samples can be investigated directly without spin dilution using proton detection...
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12-07-2021 02:05 PM
Pressure dependence of side chain 1 H and 15 N-chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Pressure dependence of side chain 1 H and 15 N-chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Abstract
For interpreting the pressure induced shifts of resonance lines of folded as well as unfolded proteins the availability of data from well-defined model systems is indispensable. Here, we report the pressure dependence of 1H and 15N chemical shifts of the side chain atoms in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (Xxx is one of the 20 canonical amino acids) measured at 800Â*MHz proton frequency. As observed earlier for other...
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06-22-2020 10:19 PM
Pressure dependence of side chain 13 C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Pressure dependence of side chain 13 C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Abstract
For evaluating the pressure responses of folded as well as intrinsically unfolded proteins detectable by NMR spectroscopy the availability of data from well-defined model systems is indispensable. In this work we report the pressure dependence of 13C chemical shifts of the side chain atoms in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (Xxx, one of the 20 canonical amino acids). Contrary to expectation the chemical shifts of a number of...
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09-14-2017 11:59 AM
Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Abstract
For a better understanding of nuclear magnetic resonance (NMR) detected pressure responses of folded as well as unstructured proteins the availability of data from well-defined model systems are indispensable. In this work we report the pressure dependence of chemical shifts of the backbone atoms 1Hα, 13Cα and 13C� in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (Xxx one of the 20 canonical amino acids). Contrary to...
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06-22-2016 09:14 PM
Deuterium isotope shifts for backbone 1H, 15N and 13C nuclei in intrinsically disordered protein α-synuclein
Deuterium isotope shifts for backbone 1H, 15N and 13C nuclei in intrinsically disordered protein α-synuclein
Abstract Intrinsically disordered proteins (IDPs) are abundant in nature and characterization of their potential structural propensities remains a widely pursued but challenging task. Analysis of NMR secondary chemical shifts plays an important role in such studies, but the output of such analyses depends on the accuracy of reference random coil chemical shifts. Although uniform perdeuteration of IDPs can dramatically increase spectral resolution, a feature particularly...
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09-10-2012 01:48 AM
[NMR paper] A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR
A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR experiment and quantum chemical calculations.
Related Articles A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR experiment and quantum chemical calculations.
J Biomol NMR. 2005 Feb;31(2):87-95
Authors: Ko?mi?ski W, Zhukov I, Pecul M, Sadlej J
A new pulse sequence exploiting double- and zero-quantum evolution of two-spin 15N-13C' coherence is proposed for the accurate measurements of 2J(N(i),C alpha(i-1)) coupling...
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11-24-2010 11:14 PM
[NMR paper] Temperature-dependence of protein hydrogen bond properties as studied by high-resolut
Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR.
Related Articles Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR.
J Mol Biol. 2002 Apr 12;317(5):739-52
Authors: Cordier F, Grzesiek S
The temperature-dependence of a large number of NMR parameters describing hydrogen bond properties in the protein ubiquitin was followed over a range from 5 to 65 degrees C. The parameters comprise hydrogen bond (H-bond) scalar couplings, h3JNC', chemical shifts, amide...
NMR detection and conformational dependence of two, three, and four-bond isotope shifts due to deuteration of backbone amides
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