Zobrazeno 1 - 10
of 1 362
pro vyhledávání: '"J H, Prestegard"'
Autor:
Beriashvili D; NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padaulaan 8, 3584 CH, Utrecht, The Netherlands., Folkers GE; NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padaulaan 8, 3584 CH, Utrecht, The Netherlands., Baldus M; NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padaulaan 8, 3584 CH, Utrecht, The Netherlands.
Publikováno v:
Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Dec 16; Vol. 25 (24), pp. e202400508. Date of Electronic Publication: 2024 Oct 17.
Autor:
Hunter CD; Department of Chemistry, University of Alberta, Edmonton, Alberta, T6G 2G2, Canada., Cairo CW; Department of Chemistry, University of Alberta, Edmonton, Alberta, T6G 2G2, Canada.
Publikováno v:
Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Dec 02; Vol. 25 (23), pp. e202400402. Date of Electronic Publication: 2024 Oct 23.
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::495839914844d3c01a245cead212fe72
https://doi.org/10.1021/j100140a048
https://doi.org/10.1021/j100140a048
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ce304d4aa2354ee341c13e8bc82151d
https://doi.org/10.1021/bi00154a003
https://doi.org/10.1021/bi00154a003
Autor:
Franz AH; Department of Chemistry, University of the Pacific, Stockton, California, USA., Bromley KS; Department of Chemistry, University of the Pacific, Stockton, California, USA., Aung ET; Department of Chemistry, University of the Pacific, Stockton, California, USA., Do SQL; Department of Chemistry, University of the Pacific, Stockton, California, USA., Rosenblatt HM; Department of Chemistry, University of the Pacific, Stockton, California, USA., Watson AJ; Department of Chemistry, University of the Pacific, Stockton, California, USA.
Publikováno v:
Magnetic resonance in chemistry : MRC [Magn Reson Chem] 2025 Jan; Vol. 63 (1), pp. 3-16. Date of Electronic Publication: 2024 Oct 16.
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb9dca47cad7a39af8e52f79d602e02d
https://doi.org/10.1021/bi00475a017
https://doi.org/10.1021/bi00475a017
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e348d12e76830ddd6a920aca7c1b3d0c
https://pubmed.ncbi.nlm.nih.gov/11061225
https://pubmed.ncbi.nlm.nih.gov/11061225
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6d238cd476a22c2585c1625e88162724
https://pubmed.ncbi.nlm.nih.gov/10605087
https://pubmed.ncbi.nlm.nih.gov/10605087
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ce33e2843475cbfcfc0a3a06cb50a69b
https://pubmed.ncbi.nlm.nih.gov/10441154
https://pubmed.ncbi.nlm.nih.gov/10441154