Zobrazeno 1 - 10
of 55
pro vyhledávání: '"J H, Prestegard"'
Autor:
J. Chung, J. H. Prestegard
Publikováno v:
The Journal of Physical Chemistry. 97:9837-9843
Anisotropic water diffusion in three lyotropic liquid-crystal systems, cesium perfluorooctanoate (CsPFO)/D 2 O, dimyristoylphosphatidylcholine (DMPC)/CHAPSO/D 2 O, and DMPC/Triton X-100/D 2 O, has been measured using the NMR pulsed field gradient spi
Publikováno v:
Biochemistry. 31:9339-9349
Transferred nuclear Overhauser effect (TRNOE) experiments have revealed a change in the torsion angles about the alpha-1-6 glycosidic bond of methyl beta-melibioside upon binding of the melibioside to the ricin B-chain (Rb). A full relaxation rate ma
Publikováno v:
Biochemistry. 29:5529-5537
Spin simulation and selective deuteration have been used to aid in the interpretation of 1D transferred nuclear Overhauser effect (TRNOE) NMR experiments on ricin B-chain/ligand systems. Application of these methods has revealed a change in the confo
Publikováno v:
eMagRes
The sections in this article are 1 Introduction 2 Transferred NOE Studies 3 Residual Dipolar Coupling Studies 4 Acknowledgements 5 Biographical Sketches
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6b9d58a67edf2578c55b8042565ad7dd
https://doi.org/10.1002/9780470034590.emrstm0480
https://doi.org/10.1002/9780470034590.emrstm0480
Publikováno v:
Journal of biomolecular NMR. 18(1)
An intensity-based constant-time COSY (CT-COSY) method is described for measuring 1H-1H residual dipolar couplings of proteins in weakly aligned media. For small proteins, the overall sensitivity of this experiment is comparable to the NOESY experime
Publikováno v:
Journal of biomolecular NMR. 15(2)
Residual dipolar couplings are being increasingly used as structural constraints for NMR studies of biomolecules. A problem arises when dipolar coupling contributions are larger than scalar contributions for a given spin pair, as is commonly observed
Publikováno v:
Biochemistry. 38(32)
The backbone dynamics of the N-terminal domain of the chaperone protein Escherichia coli DnaJ have been investigated using steady-state 1H-15N NOEs, 15N T1, T2, and T1 rho relaxation times, steady-state 13C alpha-13CO NOEs, and 13CO T1 relaxation tim
Autor:
J A, Losonczi, J H, Prestegard
Publikováno v:
Journal of biomolecular NMR. 12(3)
Dissolving biological macromolecules in dilute bicelle solutions, which form oriented liquid crystals in the presence of a magnetic field, permits measurement of anisotropic spin interactions such as dipolar couplings [Tjandra, N. and Bax, A., Scienc
Autor:
R, Ghose, J H, Prestegard
Publikováno v:
Journal of magnetic resonance (San Diego, Calif. : 1997). 134(2)
We have investigated the underlying assumptions in estimating cross-correlation rates between chemical shift anisotropy (CSA) and dipolar coupling mechanisms in a scalar-coupled two-spin IS system, from laboratory frame relaxation experiments. It has
Publikováno v:
Journal of biomolecular NMR. 12(2)
We present heteronuclear two-dimensional methods for the analysis of the geometry of exchangeable protons on a protein-bound carbohydrate. By using a water-selective NOESY-HSQC, we observed cross-relaxation between carbohydrate hydroxyl protons and n