K V Pervushin
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Explore the profile of K V Pervushin including associated specialties, affiliations and a list of published articles.
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13
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283
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Recent Articles
1.
Pervushin K, Orekhov V, Korzhnev D, Arseniev A
J Biomol NMR
. 2012 Aug;
5(4):383-96.
PMID: 22911558
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...
2.
Orekhov V, Pervushin K, Korzhnev D, Arseniev A
J Biomol NMR
. 2012 Aug;
6(2):113-22.
PMID: 22910799
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...
3.
Pervushin K, Wider G, Wuthrich K
J Biomol NMR
. 2010 Dec;
12(2):345-8.
PMID: 21136330
This paper describes the use of single transition-to-single transition polarization transfer (ST2-PT) in transverse relaxation-optimized spectroscopy (TROSY), where it affords a [Formula: see text] sensitivity enhancement for kinetically stable amide...
4.
Orekhov V, Korzhnev D, Pervushin K, Hoffmann E, Arseniev A
J Biomol Struct Dyn
. 1999 Sep;
17(1):157-74.
PMID: 10496429
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...
5.
Pervushin K, Wider G, Riek R, Wuthrich K
Proc Natl Acad Sci U S A
. 1999 Aug;
96(17):9607-12.
PMID: 10449740
In our 3D NOESY-[(1)H,(15)N,(1)H]-ZQ-TROSY experiment, the TROSY principle (transverse relaxation-optimized spectroscopy) is used in three-dimensional (3D) (15)N-resolved nuclear Overhauser enhancement spectroscopy (NOESY), which enables resonance assignments by sequential nuclear Overhauser...
6.
Luginbuhl P, Pervushin K, Iwai H, Wuthrich K
Biochemistry
. 1997 Jun;
36(24):7305-12.
PMID: 9200679
The backbone dynamics of the uniformly 15N-labeled N-terminal 63-residue DNA-binding domain of the 434 repressor has been characterized by measurements of the individual 15N longitudinal relaxation times, T1, transverse relaxation...
7.
Pervushin K, Arsenev A
Bioorg Khim
. 1995 Feb;
21(2):83-111.
PMID: 7748211
The review covers the field of the spatial structure determination of membrane-associated peptides and proteins by the High-Resolution NMR Spectroscopy. The membrane-bound conformations of several hormones, neuropeptides, lipopeptides, peptide antibiotics,...
8.
Orekhov VYu , Pervushin K, Arseniev A
Eur J Biochem
. 1994 Feb;
219(3):887-96.
PMID: 8112340
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...
9.
Pervushin K, Orekhov VYu , Popov A, Musina LYu , Arseniev A
Eur J Biochem
. 1994 Jan;
219(1-2):571-83.
PMID: 8307023
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...
10.
Pervushin K, Sobol A, Musina L, Abdulaeva G, Arsenev A
Mol Biol (Mosk)
. 1992 Nov;
26(6):1397-415.
PMID: 1491681
Spatial structures of proteolytic segment A (sA) of bacterioopsin of Halobacterium halobium (residues 1-36) solubilized in the mixture of methanol-chloroform (1:1), 0.1 M LiClO4 or in perdeuteriated sodium dodecyl sulfate...