Deuterium Quadrupole-Coupling and Chemical-Shielding Tensors in the Model Dipeptide Glycylglycine Monohydrochloride Monohydrate

Michal, Carl A.; Wehman, Jacqueline; Jelinski, Lynn W.

doi:10.1006/jmrb.1996.0057

Cited by 21 publications

(22 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…19 Some additional NMR data on the C-C distances are available, and this also agrees with the diffraction structure. 20 Gly-Gly-Gly-HCl has one more peptide bond and so it should show three N-D stretch bands from the amino group and two peptide N-D stretches.…”

Section: Glycylglycine Hydrochloridesupporting

confidence: 59%

Infrared Hole Burning of the Amino Group in Amino Acid and Peptide Salts

Strauss

2001

J. Phys. Chem. B

View full text Add to dashboard Cite

Monodeuterated derivatives of the salts of tyrosine, valine, glycylglycine, and glycylglycylglycine are investigated by infrared spectroscopy. Irradiation in the spectral region of the N-D stretch bands produces spectral holes and antiholes. These result from rotation of N-D-containing moieties. The holes and antiholes identify the vibrations of the amino group and provide information on the hydrogen-bonding environment. Both the various amino acid salts and the two peptide salts hole burn, suggesting that infrared hole burning will provide a useful tool for investigating a range of biologically interesting materials.

show abstract

Section: Glycylglycine Hydrochloridesupporting

confidence: 59%

Infrared Hole Burning of the Amino Group in Amino Acid and Peptide Salts

Strauss

2001

J. Phys. Chem. B

View full text Add to dashboard Cite

show abstract

“…Application of one or a series of 180°pulses on spin I during the evolution of spin S interchanges the slowly and rapidly relaxing components of the S multiplet, which results in averaging of the slow and fast relaxation rates and elimination of the CSA͞DD interference (25,26 (Fig. 3 a1 and b1) (27) and for ⌬ N of Ϫ160 ppm (28) were determined. Independently, solution NMR experiments yielded values for ⌬ H of backbone amide protons in the range 3 to 15 ppm (37) and ⌬ N near Ϫ170 ppm (10).…”

Section: Resultsmentioning

confidence: 99%

Attenuated T ₂ relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Pervushin¹,

Riek²,

Wider³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

2,343

1,818

View full text Add to dashboard Cite

NMR spectroscopy with proteins based on observation of a small number of spins with outstanding spectral properties, which either may be present naturally or introduced by techniques such as site-specific isotope labeling, yielded biologically relevant information on human hemoglobin (M ϭ 65,000) as early as 1969 (1), and subsequently also for significantly larger systems such as Igs (2). In contrast, the use of NMR for de novo structure determination (3, 4) so far has been limited to relatively small molecular sizes, with the largest NMR structure below molecular weight 30,000. Although NMR in structural biology may, for practical reasons of coordinated use with x-ray crystallography (5), focus on smaller molecular sizes also in the future, considerable effort goes into attempts to extend the size limit to bigger molecules (for example, see refs. 6-8). Here we introduce transverse relaxation-optimized spectroscopy (TROSY) and present experimental data and theoretical considerations showing that this approach is capable of significantly reducing transverse relaxation rates and thus overcomes a key obstacle opposing solution NMR of larger molecules (7).At the high magnetic fields typically used for studies of proteins and nucleic acids, chemical shift anisotropy interaction (CSA) of 1 H, 15 N, and 13 C nuclei forms a significant source of relaxation in proteins and nucleic acids, in addition to dipole-dipole (DD) relaxation. This leads to increase of the overall transverse relaxation rates with increasing polarizing magnetic field, B 0 . Nonetheless, transverse relaxation of amide protons in larger proteins at high fields has been reduced successfully by complete or partial replacement of the nonlabile hydrogen atoms with deuterons and, for example, more than 90% of the 15 N, 13 C ␣ , and 1 H N chemical shifts thus were assigned in the polypeptide chains of a protein-DNA complex of size 64,000 (6). TROSY uses spectroscopic means to further reduce T 2 relaxation based on the fact that cross-correlated relaxation caused by DD and CSA interference gives rise to different relaxation rates of the individual multiplet components in a system of two coupled spins 1 ⁄2, I and S, such as the 15 N-1 H fragment of a peptide bond (9, 10). Theory shows that at 1 H frequencies near 1 GHz nearly complete cancellation of all transverse relaxation effects within a 15 N-1 H moiety can be achieved for one of the four multiplet components. TROSY observes exclusively this narrow component, for which the residual linewidth is then almost entirely because of DD interactions with remote hydrogen atoms in the protein. These can be efficiently suppressed by 2 H-labeling, so that in TROSY-type experiments the accessible molecular size for solution NMR studies no longer is primarily limited by T 2 relaxation. TheoryWe consider a system of two scalar coupled spins 1 ⁄2, I and S, with a scalar coupling constant J IS , which is located in a protein molecule. T 2 relaxation of this spin system is dominated by the DD coupling of I and S a...

show abstract

“…It corresponds to only one-hundredth of the linewidth and to only one-twentieth of the digital resolution δν dig . Essentially the same procedure for locating resonances as used here was adopted in (22). The authors estimate that their precision is about 50 Hz.…”

Section: Preparatory Testsmentioning

confidence: 98%

“…Hence, the only method for getting deuteron bond directions with sufficient accuracy to test rule (ii) meaningfully is neutron diffraction. Still, we are not aware of any case where a nonzero deviation of e b and e Z outside the combined error limits of the neutron diffraction and NMR experiments has been found (note, we are not talking of deuterons in hydrogen bonds where such deviations have at least been claimed (21,22)). …”

Section: Introductionmentioning

confidence: 94%

Precision Measurement of the Quadrupole Coupling and Chemical Shift Tensors of the Deuterons in α-Calcium Formate

Schmitt

Zimmermann

Körner

et al. 2001

Journal of Magnetic Resonance

View full text Add to dashboard Cite

Deuterium Quadrupole-Coupling and Chemical-Shielding Tensors in the Model Dipeptide Glycylglycine Monohydrochloride Monohydrate

Cited by 21 publications

References 13 publications

Infrared Hole Burning of the Amino Group in Amino Acid and Peptide Salts

Infrared Hole Burning of the Amino Group in Amino Acid and Peptide Salts

Attenuated T ₂ relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Precision Measurement of the Quadrupole Coupling and Chemical Shift Tensors of the Deuterons in α-Calcium Formate

Contact Info

Product

Resources

About

Deuterium Quadrupole-Coupling and Chemical-Shielding Tensors in the Model Dipeptide Glycylglycine Monohydrochloride Monohydrate

Cited by 21 publications

References 13 publications

Infrared Hole Burning of the Amino Group in Amino Acid and Peptide Salts

Infrared Hole Burning of the Amino Group in Amino Acid and Peptide Salts

Attenuated T 2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Precision Measurement of the Quadrupole Coupling and Chemical Shift Tensors of the Deuterons in α-Calcium Formate

Contact Info

Product

Resources

About

Attenuated T ₂ relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution