Finkelstein AV - Search Results

1

Correction: Finkelstein et al. How Can Ice Emerge at 0 °C? Biomolecules 2022, 12, 981.

Finkelstein AV, Garbuzynskiy SO, Melnik BS. Finkelstein AV, et al. Biomolecules. 2023 Nov 23;13(12):1687. doi: 10.3390/biom13121687. Biomolecules. 2023. PMID: 38136677 Free PMC article.

2

Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics.

Galzitskaya OV, Garbuzynskiy SO, Ivankov DN, Finkelstein AV. Galzitskaya OV, et al. Among authors: finkelstein av. Proteins. 2003 May 1;51(2):162-6. doi: 10.1002/prot.10343. Proteins. 2003. PMID: 12660985

3

Contact order revisited: influence of protein size on the folding rate.

Ivankov DN, Garbuzynskiy SO, Alm E, Plaxco KW, Baker D, Finkelstein AV. Ivankov DN, et al. Among authors: finkelstein av. Protein Sci. 2003 Sep;12(9):2057-62. doi: 10.1110/ps.0302503. Protein Sci. 2003. PMID: 12931003 Free PMC article.

4

Outlining folding nuclei in globular proteins.

Garbuzynskiy SO, Finkelstein AV, Galzitskaya OV. Garbuzynskiy SO, et al. Among authors: finkelstein av. J Mol Biol. 2004 Feb 13;336(2):509-25. doi: 10.1016/j.jmb.2003.12.018. J Mol Biol. 2004. PMID: 14757062

5

Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?

Garbuzynskiy SO, Melnik BS, Lobanov MY, Finkelstein AV, Galzitskaya OV. Garbuzynskiy SO, et al. Among authors: finkelstein av. Proteins. 2005 Jul 1;60(1):139-47. doi: 10.1002/prot.20491. Proteins. 2005. PMID: 15856480

6

Three-state protein folding: experimental determination of free-energy profile.

Baryshnikova EN, Melnik BS, Finkelstein AV, Semisotnov GV, Bychkova VE. Baryshnikova EN, et al. Among authors: finkelstein av. Protein Sci. 2005 Oct;14(10):2658-67. doi: 10.1110/ps.051402705. Epub 2005 Sep 9. Protein Sci. 2005. PMID: 16155199 Free PMC article.

7

Understanding the folding rates and folding nuclei of globular proteins.

Finkelstein AV, Ivankov DN, Garbuzynskiy SO, Galzitskaya OV. Finkelstein AV, et al. Curr Protein Pept Sci. 2007 Dec;8(6):521-36. doi: 10.2174/138920307783018695. Curr Protein Pept Sci. 2007. PMID: 18220841 Review.

8

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: finkelstein av. Protein Sci. 2009 Oct;18(10):2152-9. doi: 10.1002/pro.229. Protein Sci. 2009. PMID: 19693934 Free PMC article.

9

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: finkelstein av. 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.

10

Golden triangle for folding rates of globular proteins.

Garbuzynskiy SO, Ivankov DN, Bogatyreva NS, Finkelstein AV. Garbuzynskiy SO, et al. Among authors: finkelstein av. Proc Natl Acad Sci U S A. 2013 Jan 2;110(1):147-50. doi: 10.1073/pnas.1210180110. Epub 2012 Dec 18. Proc Natl Acad Sci U S A. 2013. PMID: 23251035 Free PMC article.

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