Search Results - "Semisotnov, G. V"

Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe by Semisotnov, G V, Rodionova, N A, Razgulyaev, O I, Uversky, V N, Gripas', A F, Gilmanshin, R I

“…Binding of the hydrophobic fluorescent probe, 1-anilino-naphthalene-8-sulfonate (ANS), to synthetic polypeptides and proteins with a different structural…”
Get more information

Refolding of scFv mini-antibodies using size-exclusion chromatography via arginine solution layer by Fursova, K.K., Laman, A.G., Melnik, B.S., Semisotnov, G.V., Kopylov, P.Kh, Kiseleva, N.V., Nesmeyanov, V.A., Brovko, F.A.

“…The method for refolding of mini-antibodies using size-exclusion chromatography via arginine solution layer was developed. This method allows to refold scFv,…”
Get full text

The Molten Globule Concept: 45 Years Later by Bychkova, V. E., Semisotnov, G. V., Balobanov, V. A., Finkelstein, A. V.

“…In this review, we describe traditional systems where the molten globule (MG) state has been detected and give a brief description of the solution of…”
Get full text

Molecular chaperone GroEL/ES: Unfolding and refolding processes by Ryabova, N. A., Marchenkov, V. V., Marchenkova, S. Yu, Kotova, N. V., Semisotnov, G. V.

“…Molecular chaperones are a special class of heat shock proteins (Hsp) that assist the folding and formation of the quaternary structure of other proteins both…”
Get full text

Evidence for a molten globule state as a general intermediate in protein folding by Ptitsyn, O.B., Pain, R.H., Semisotnov, G.V., Zerovnik, E., Razgulyaev, O.I.

“…The folding of globular proteins occurs through intermediate states whose characterisation provides information about the mechanism of folding. A major class…”
Get full text

Temperature-induced conformational transitions of the glucanotransferase Bgl2p isolated from Saccharomyces cerevisiae cell walls by Bezsonov, E. E, Kalebina, T. S, Gorkovskii, A. A, Kudryashova, I. B, Semisotnov, G. V, Kulaev, I. S

Get full text

Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy by Ryabova, N. A., Selivanova, O. M., Semisotnov, G. V.

“…The products of the reassembly reaction of tetradecameric two-ring quaternary structure of GroEL chaperonin under the pressure of its heptameric co-chaperonin…”
Get full text

Affinity chromatography of chaperones based on denatured proteins: Analysis of cell lysates of different origin by Marchenko, N. Yu, Sikorskaya, E.V., Marchenkov, V.V., Kashparov, I.A., Semisotnov, G.V.

“…Molecular chaperones are involved in folding, oligomerization, transport, and degradation of numerous cellular proteins. Most of chaperones are heat-shock…”
Get full text

Limited Trypsinolysis of GroES: The Effect on the Interaction with GroEL and Assembly In Vitro by Marchenkov, V. V., Kotova, N. V., Muranova, T. A., Semisotnov, G. V.

“…GroES is a heptameric partner of tetradecameric molecular chaperone GroEL, which ensures the correct folding and assembly of numerous cellular proteins both in…”
Get full text

‘All-or-none’ mechanism of the molten globule unfolding by Uversky, V.N., Semisotnov, G.V., Pain, R.H., Ptitsyn, O.B.

“…The Gdm-HCl-induced unfolding of bovine carbonic anhydrase B and S. aureus β-lactamase was studied at 4°C by a variety of methods. With the use of FPLC it has…”
Get full text

On the role of some conserved and nonconserved amino acid residues in the transitional state and intermediate of apomyoglobin folding by Baryshnikova (Samatova), E. N, Melnik, B. S, Balobanov, V. A, Katina, N. S, Finkelshtein, A. V, Semisotnov, G. V, Bychkova, V. E

“…The contributions of some amino acid residues in the A, B, G, and H helices to the formation of the folding nucleus and folding intermediate of apomyoglobin…”
Get full text

GroES co-chaperonin small-angle X-ray scattering study shows ring orifice increase in solution by Timchenko, A.A., Melnik, B.S., Kihara, H., Kimura, K., Semisotnov, G.V.

“…GroES consists of seven identical 10 kDa subunits and is involved in assisting protein folding as the partner of another oligomeric protein, the GroEL…”
Get full text

Sequential mechanism of refolding of carbonic anhydrase B by Semisotnov, Gennady V., Rodionova, Natalya A., Kutyshenko, Victor P., Ebert, Bernd, Blanck, Jürgen, Ptitsyn, Oleg B.

“…The kinetics of refolding of bovine carbonic anhydrase B was studied by a variety of methods over a wide range of times (from milliseconds to hours). It has…”
Get full text

Dataset concerning GroEL chaperonin interaction with proteins by Marchenkov, V.V., Marchenko, N.Yu, Kaysheva, A.L., Kotova, N.V., Kashparov, I.A., Semisotnov, G.V.

“…GroEL chaperonin is well-known to interact with a wide variety of polypeptide chains. Here we show the data related to our previous work…”
Get full text

α-lactalbumin: compact state with fluctuating tertiary structure? by Dolgikh, D.A., Gilmanshin, R.I., Brazhnikov, E.V., Bychkova, V.E., Semisotnov, G.V., Venyaminov, S.Yu, Ptitsyn, O.B.

Get full text

Ligands regulate GroEL thermostability by Surin, A.K, Kotova, N.V, Kashparov, I.A, Marchenkov, V.V, Marchenkova, S.Yu, Semisotnov, G.V

“…Escherichia coli heat-shock proteins GroEL and GroES stimulate (in an ATP-dependent manner) the folding of various proteins. In this study scanning…”
Get full text

Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization by Semisotnov, G V, Uversky, V N, Sokolovsky, I V, Gutin, A M, Razgulyaev, O I, Rodionova, N A

“…Kinetics of refolding of bovine carbonic anhydrase B have been studied by the "double-jump" technique (i.e. the dependence of protein refolding on delay time…”
Get more information

Affinity chromatography of GroEL chaperonin based on denatured proteins: role of electrostatic interactions in regulation of GroEL affinity for protein substrates by Marchenko, N Iu, Marchenkov, V V, Kaĭsheva, A L, Kashparov, I A, Kotova, N V, Kaliman, P A, Semisotnov, G V

“…The chaperonin GroEL of the heat shock protein family from Escherichia coli cells can bind various polypeptides lacking rigid tertiary structure and thus…”
Get full text

Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy by Arai, M, Ikura, T, Semisotnov, G.V, Kihara, H, Amemiya, Y, Kuwajima, K

“…beta-Lactoglobulin (beta LG) is a predominantly beta-sheet protein with a markedly high helical propensity and forms non-native alpha-helical intermediate in…”
Get full text

Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin by Dolgikh, D A, Abaturov, L V, Bolotina, I A, Brazhnikov, E V, Bychkova, V E, Gilmanshin, R I, Lebedev YuO, Semisotnov, G V, Tiktopulo, E I, Ptitsyn, O B

“…We describe a novel physical state of a protein molecule which is nearly as compact as the native state and has pronounced secondary structure, but differs…”
Get full text