Zobrazeno 1 - 10
of 207
pro vyhledávání: '"Oleg Jardetzky"'
Autor:
Oleg Jardetzky
Publikováno v:
Journal of Magnetic Resonance. 206:2-8
The early history of the principal meeting in the field of biological NMR spectroscopy, the International Conference on Magnetic Resonance in Biological Systems (ICMRBS), is presented from the perspective of one of the founders.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ea88dd2df398b0c91d7972aa7260d55
https://doi.org/10.1016/j.jmr.2010.07.005
https://doi.org/10.1016/j.jmr.2010.07.005
Autor:
Oleg Jardetzky, Yunjun Wang
Publikováno v:
Journal of Biomolecular NMR. 28:327-340
Empirical shielding surfaces are most commonly used to predict chemical shifts in proteins from known backbone torsion angles, phi and psi. However, the prediction of (15)N chemical shifts using this technique is significantly poorer, compared to tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfe4cb0ad2608693566f8a546a779d11
https://doi.org/10.1023/b:jnmr.0000015397.82032.2a
https://doi.org/10.1023/b:jnmr.0000015397.82032.2a
Publikováno v:
ACS Symposium Series. :xiii-xxviii
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2f65956f8a98cfead47a07634af5cc7b
https://doi.org/10.1021/bk-2002-0827.pr001
https://doi.org/10.1021/bk-2002-0827.pr001
Autor:
Oleg Jardetzky, Yunjun Wang
Publikováno v:
Protein Science. 11:852-861
For a long time, NMR chemical shifts have been used to identify protein secondary structures. Currently, this is accomplished through comparing the observed (1)H(alpha), (13)C(alpha), (13)C(beta), or (13)C' chemical shifts with the random coil values
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f755ba96c348696de30e34729c417dc
https://doi.org/10.1110/ps.3180102
https://doi.org/10.1110/ps.3180102
Autor:
Oleg Jardetzky, Jean-François Lefèvre
This volume is a collection of articles from the proceedings of the International School of Structural Biology and Magnetic Resonance 3rd Course: Protein Dynamics, Function, and Design. This NATO Advance Study Institute was held in Erice at the Ettor
Autor:
Oleg Jardetzky, Jean-François Lefèvre
From within complex structures of organisms and cells down to the molecular level, biological processes all involve movement. Muscular fibers slide on each other to activate the muscle, as polymerases do along nucleic acids for replicating and transc
Autor:
Oleg Jardetzky, Michael D. Finucane
Publikováno v:
Molecular Physics. 95:1127-1136
The Linderstr⊘m-Lang model describes proton exchange as proceeding from an ‘open’ state which is in equilibrium with a ‘closed’ state from which exchange cannot occur. This predicts a biexponential exchange process, although limiting condit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d6e78a3fa8dd728944d86e2b06a60354
https://doi.org/10.1080/00268979809483244
https://doi.org/10.1080/00268979809483244
Autor:
Michael D. Finucane, Oleg Jardetzky
Publikováno v:
Protein Science. 5:653-662
The pH dependence of amide proton exchange rates have been measured for trp-repressor. One class of protons exchanges too fast to be measured in these experiments. Among the protons that have measurable hydrogen-deuterium exchange rates, two addition
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef6da6b8500ecc1f27962fc0f62575ce
https://doi.org/10.1002/pro.5560050409
https://doi.org/10.1002/pro.5560050409
Publikováno v:
Biochemistry. 34:13183-13189
Binding of L-tryptophan to Escherichia coli trp repressor wild type (WT) and AV77 mutant was studied by 1H NMR spectroscopy. Ligand binding to the proteins resulted in changes in line widths and chemical shifts of ligand resonances, but no changes in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3ca64061a7edf7306632422e7b5356f
https://doi.org/10.1021/bi00040a033
https://doi.org/10.1021/bi00040a033
Publikováno v:
Protein & Peptide Letters. 1:120-127
We have investigated the characteristics of high B-factor (disordered) regions within otherwise well-resolved protein structures. We find that amino acids K, S, Q, A, D, E, P, N, D, and R occur more frequently in disordered regions, 40% of disordered
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::64a3e0c2fc90e09915d3442c69b0caa7
https://doi.org/10.2174/0929866501666220424143724
https://doi.org/10.2174/0929866501666220424143724