Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Konstantine V. Pervushin"'
Publikováno v:
Applied Magnetic Resonance. 3:965-973
An interactive technique for the evaluation of cross-peak volumes in 2D-spectra is presented, based on a 1D nonlinear curve-fitting procedure. The effects of applied window functions, truncation of time domain data and cross-peak overlap on the evalu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::477caf5ee5a1a9fa8bcf0f8c8ab3335f
https://doi.org/10.1007/bf03166166
https://doi.org/10.1007/bf03166166
Publikováno v:
Journal of Biomolecular NMR. 2:361-372
The spatial structure of a synthetic 32-residue polypeptide, an analog of the membrane-spanning segment B (residues 34-65) of bacterioopsin of Halobacterium halobium, incorporated into perdeuterated sodium dodecyl sulfate micelles, was determined fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5054480c33bba7757c4e6a4d5de67c37
https://doi.org/10.1007/bf01874814
https://doi.org/10.1007/bf01874814
Autor:
Alexander S. Arseniev, Eberhard Hoffmann, Dmitry M. Korzhnev, Vladislav Yu. Orekhov, Konstantine V. Pervushin
Publikováno v:
Journal of biomolecular structuredynamics. 17(1)
This paper presents a procedure for detection of intermediate nanosecond internal dynamics in globular proteins. The procedure uses 1H-15N relaxation measurements at several spectrometer frequencies and hydrodynamic calculations based on experimental
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c7b61f06dd91c711c6fda3125b2f7e1
https://pubmed.ncbi.nlm.nih.gov/10496429
https://pubmed.ncbi.nlm.nih.gov/10496429
Publikováno v:
Journal of biomolecular NMR. 6(2)
The backbone dynamics of uniformly (15)N-labelled fragments (residues 1-71 and 1-36) of bacterioopsin, solubilized in two media (methanol-chloroform (1:1), 0.1 M (2)HCO(2)NH(4), or SDS micelles) have been investigated using 2D proton-detected heteron
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4502da3340b76bc55cc237ae8aac58e2
https://pubmed.ncbi.nlm.nih.gov/22910799
https://pubmed.ncbi.nlm.nih.gov/22910799
Publikováno v:
Journal of biomolecular NMR. 5(4)
The influence of the internal dynamics of two polypeptides comprising transmembrane α-helix A or two α-helices A and B of bacterioopsin on experimentally accessible (15)N NMR relaxation rates was investigated by molecular dynamics (MD) simulations,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c52f07c37fc1a63dafa96b27e96ce69
https://pubmed.ncbi.nlm.nih.gov/22911558
https://pubmed.ncbi.nlm.nih.gov/22911558
Publikováno v:
European journal of biochemistry. 219(3)
The backbone dynamics of a uniformly 15N-labelled proteolytic fragment (residues 1-71) of bacteriorhodopsin, solubilized in two media [methanol/chloroform (1:1), 0.1 M 2HCO2NH4 and SDS micelles] have been investigated using two-dimensional proton-det
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1d868371373a30ecfece554731b54ac
https://pubmed.ncbi.nlm.nih.gov/8112340
https://pubmed.ncbi.nlm.nih.gov/8112340
Autor:
Larisa Yu. Musina, Konstantine V. Pervushin, Vladislav Yu. Orekhov, A. I. Popov, Alexander S. Arseniev
Publikováno v:
European journal of biochemistry. 219(1-2)
Spatial structures of a chymotryptic fragment C2 (residues 1-71) of bacterioopsin from Halobacterium halobium, solubilized in a mixture of methanol/chloroform (1:1, by vol.) and 0.1 M 2HCO2NH4, or in perdeuterated sodium (2H)dodecyl sulfate (SDS) mic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49d6a7f74bc946c4bb2c701ec475c0cb
https://pubmed.ncbi.nlm.nih.gov/8307023
https://pubmed.ncbi.nlm.nih.gov/8307023
Publikováno v:
FEBS letters. 308(2)
Spatial structures of proteolytic segment A (sA) of bacterioopsin of H. halobium (residues 1-36) solubilized in a mixture of methanol-chloroform (1:1), 0.1 M LiClO4 organic mixture, or in perdeuterated sodium dodecyl sulfate (SDS) micelles, were dete
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d64a49d217764f315cfdae5583ec237
https://pubmed.ncbi.nlm.nih.gov/1323484
https://pubmed.ncbi.nlm.nih.gov/1323484
Publikováno v:
Journal of biomolecular NMR. 1(4)
The conformation of the synthetic 32-residue polypeptide, an analog of the membrane spanning segment B (residues 34-65) of Halobacterium halobium bacterioopsin, incorporated into perdeuterated sodium dodecyl sulfate micelles in the presence of triflu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b79af68b772e6d780f5e7296f53043a
https://pubmed.ncbi.nlm.nih.gov/1841702
https://pubmed.ncbi.nlm.nih.gov/1841702