Balobanov VA - Search Results

1

How membrane surface affects protein structure.

Bychkova VE, Basova LV, Balobanov VA. Bychkova VE, et al. Among authors: balobanov va. Biochemistry (Mosc). 2014 Dec;79(13):1483-514. doi: 10.1134/S0006297914130045. Biochemistry (Mosc). 2014. PMID: 25749161 Free article. Review.

2

pH-induced equilibrium unfolding of apomyoglobin: substitutions at conserved Trp14 and Met131 and non-conserved Val17 positions.

Dyuysekina AE, Dolgikh DA, Samatova Baryshnikova EN, Tiktopulo EI, Balobanov VA, Bychkova VE. Dyuysekina AE, et al. Among authors: balobanov va. Biochemistry (Mosc). 2008 Jun;73(6):693-701. doi: 10.1134/s0006297908060102. Biochemistry (Mosc). 2008. PMID: 18620536

3

How strong are side chain interactions in the folding intermediate?

Samatova EN, Katina NS, Balobanov VA, Melnik BS, Dolgikh DA, Bychkova VE, Finkelstein AV. Samatova EN, et al. Among authors: balobanov va. Protein Sci. 2009 Oct;18(10):2152-9. doi: 10.1002/pro.229. Protein Sci. 2009. PMID: 19693934 Free PMC article.

4

Folding intermediate and folding nucleus for I-->N and U-->I-->N transitions in apomyoglobin: contributions by conserved and nonconserved residues.

Samatova EN, Melnik BS, Balobanov VA, Katina NS, Dolgikh DA, Semisotnov GV, Finkelstein AV, Bychkova VE. Samatova EN, et al. Among authors: balobanov va. Biophys J. 2010 Apr 21;98(8):1694-702. doi: 10.1016/j.bpj.2009.12.4326. Biophys J. 2010. PMID: 20409491 Free PMC article.

5

Apomyoglobin mutants with single point mutations at val10 can form amyloid structures at permissive temperature.

Katina NS, Ilyina NB, Kashparov IA, Balobanov VA, Vasiliev VD, Bychkova VE. Katina NS, et al. Among authors: balobanov va. Biochemistry (Mosc). 2011 May;76(5):555-63. doi: 10.1134/S0006297911050051. Biochemistry (Mosc). 2011. PMID: 21639835

6

An Experimental Tool to Estimate the Probability of a Nucleotide Presence in the Crystal Structures of the Nucleotide-Protein Complexes.

Nemchinova M, Balobanov V, Nikonova E, Lekontseva N, Mikhaylina A, Tishchenko S, Nikulin A. Nemchinova M, et al. Protein J. 2017 Jun;36(3):157-165. doi: 10.1007/s10930-017-9709-y. Protein J. 2017. PMID: 28317076

7

Intermediate States of Apomyoglobin: Are They Parts of the Same Area of Conformations Diagram?

Balobanov VA, Katina NS, Finkelstein AV, Bychkova VE. Balobanov VA, et al. Biochemistry (Mosc). 2017 May;82(5):625-631. doi: 10.1134/S0006297917050108. Biochemistry (Mosc). 2017. PMID: 28601072

8

The Molten Globule Concept: 45 Years Later.

Bychkova VE, Semisotnov GV, Balobanov VA, Finkelstein AV. Bychkova VE, et al. Among authors: balobanov va. Biochemistry (Mosc). 2018 Jan;83(Suppl 1):S33-S47. doi: 10.1134/S0006297918140043. Biochemistry (Mosc). 2018. PMID: 29544429 Free article. Review.

9

Loops linking secondary structure elements affect the stability of the molten globule intermediate state of apomyoglobin.

Majorina MA, Balobanov VA, Uversky VN, Melnik BS. Majorina MA, et al. Among authors: balobanov va. FEBS Lett. 2020 Oct;594(20):3293-3304. doi: 10.1002/1873-3468.13905. Epub 2020 Sep 2. FEBS Lett. 2020. PMID: 32770670 Free article.

10

[Kinetics of interaction between apomyoglobin and phospholipid membrane].

Balobanov VA, Il'ina NB, Katina NS, Kashparov IA, Dolgikh DA, Bychkova VE. Balobanov VA, et al. Mol Biol (Mosk). 2010 Jul-Aug;44(4):708-17. Mol Biol (Mosk). 2010. PMID: 20873231 Russian.

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