Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Jan M. Rydzewski"'
Autor:
Rolf Gruetter, Robin A. de Graaf, Michael Garwood, Jan M. Rydzewski, Thomas Schleich, Yanping Luo
Publikováno v:
Magnetic Resonance in Medicine. 41:676-685
Magnetic resonance spectroscopy (MRS) measurements of the lactate methyl proton in rat brain C6 glioma tissue acquired in the presence of an off- resonance irradiation field, analyzed using coupled Bloch equation formalism assuming two spin pools, de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58032cebe698e8c29c389482604e7765
https://doi.org/10.1002/(sici)1522-2594(199904)41:4<676::aid-mrm5>3.0.co
https://doi.org/10.1002/(sici)1522-2594(199904)41:4<676::aid-mrm5>3.0.co
Autor:
Dale L. Boger, Jan M. Rydzewski, David A. Case, Peggy S. Eis, Walter J. Chazin, Jarrod A. Smith
Publikováno v:
Journal of Molecular Biology. 272:237-252
The three-dimensional solution structure of duocarmycin SA in complex with d-(G1ACTAATTGAC11)·d-(G12TCATT A GTC22) has been determined by restrained molecular dynamics and relaxation matrix calculations using experimental NOE distance and torsion an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::012ae70d00791eb8ffb0fe99588e453d
https://doi.org/10.1006/jmbi.1997.1223
https://doi.org/10.1006/jmbi.1997.1223
Publikováno v:
Experimental Eye Research. 56:305-316
The motional dynamics of lens proteins were studied by two 13C nuclear magnetic resonance (NMR) techniques sensitive to molecular motion to define the effect of lens water content on the presence of solid-like protein domains in ocular lenses from bo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::154c081cb47accfb2ad382b5356bf1a0
https://doi.org/10.1006/exer.1993.1040
https://doi.org/10.1006/exer.1993.1040
Publikováno v:
Journal of Magnetic Resonance (1969). 95:558-566
The formalism for off resonance rotating-frame spin-lattice relaxation was extended to include the effects of nuclear-spin magnetization transfer between two sites (A ⇆ B) in which either partial or complete saturation occurs as a consequence of of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0ba76103b28061643f7275be2c4cb9f4
https://doi.org/10.1016/0022-2364(91)90169-t
https://doi.org/10.1016/0022-2364(91)90169-t
Publikováno v:
Nucleic acids research. 24(7)
A complex between d(GGGAAAAACGG).d(CCGTTTTTCCC) and the minor groove binding drug SN-6999 has been studied by 1H nuclear magnetic resonance spectroscopy. The drug is found to bind in the d(A)5 tract, but with interactions extending one residue in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dfce0176f729402b3c2b4cbed2e56da
https://pubmed.ncbi.nlm.nih.gov/8614632
https://pubmed.ncbi.nlm.nih.gov/8614632
Publikováno v:
In Vivo Spectroscopy ISBN: 9781475794793
The off-resonance rotating frame spin-lattice relaxation experiment represents a class of magnetic resonance techniques in which a low-power, continuous-wave radiofrequency (RF) field is applied off-resonance from a selected resonance. Application of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f14e5b6575cd1a7d0b545e6f334881b6
https://doi.org/10.1007/978-1-4757-9477-9_2
https://doi.org/10.1007/978-1-4757-9477-9_2
Publikováno v:
Experimental Eye Research. 55:123
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3fff6f706d3952d6a420cea67dda858a
https://doi.org/10.1016/0014-4835(92)90650-h
https://doi.org/10.1016/0014-4835(92)90650-h
Publikováno v:
Experimental eye research. 49(3)
Proton pulsed gradient spin-echo (PGSE) nuclear magnetic resonance (NMR) spectroscopy was used to explore the free and restricted non-Brownian nature of lens water self-diffusion in calf lens tissue. At all temperatures investigated the water self-di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88a7d32dd34f3c6db994db7f9158c9ff
https://pubmed.ncbi.nlm.nih.gov/2792234
https://pubmed.ncbi.nlm.nih.gov/2792234