1. Berezovskii, I.N. & Tumanyan, V.G.
Objective method for isolating the domains of globular proteins.
Biophysics 40, 1181-1187 (1995)
1997
2. Berezovsky, I.N., Kilosanidze, G.T., Tumanyan, V.G. & Kisselev,
L.
COOH-decamers in proteins are non-random.
FEBS Letters 404, 140-142 (1997) PDF
3. Berezovskii, I.N., Esipova, N.G. & Tumanyan, V.G.
Isolation of the energy-significant parts of the globule and the
hierarchy of the domain structure of the protein macromolecule.
Biophysics 42, 557-565 (1997)
4. Berezovsky, I.N., Tumanyan, V.G. & Esipova, N.G.
Representation of amino acid sequence in terms of interaction
energy in protein globule.
FEBS Letters 418, 43-46 (1997) PDF
1998
5. Berezovskii, I.N., Esipova, N.G. & Tumanyan, V.G.
Spatial distribution of directed interactions in globular protein structures.
Biophysics 43, 367-377 (1998) PDF
6. Berezovskii, I.N., Esipova, N.G., Tumanyan, V.G. & Namiot, V.A.
A new
approach to calculating of van der Waals interaction energies
in protein macromolecules.
Dielectric constant as a physical parameter.
Biophysics 43, 909-916 (1998) PDF
1999
7. Berezovsky, I.N., Kilosanidze, G.T., Tumanyan, V.G. & Kisselev,
L.L.
Amino
acid composition of protein termini are biased in different manner.
Protein Engineering 12, 23-30 (1999) PDF
8. Berezovsky, I.N., Namiot, V.A., Tumanyan, V.G. & Esipova, N.G.
Hierarchy
of the interaction energy distribution in the spatial structure
of globular
proteins and the problem of domain definition.
J. Biomol. Struct. Dyn. 17, 133-155 (1999) PDF
2000
9. Berezovsky, I.N., Grosberg, A.Y. & Trifonov, E.N.
Closed
loops of nearly standard size: common basic element of protein structure.
FEBS Letters 466, 283-286 (2000) PDF
10. Berezovsky, I.N., Esipova, N.G., Tumanyan, V.G. & Namiot, V.A.
A new approach for the calculation of the energy of van der Waals
interactions in macromolecules of globular proteins.
J. Biomol. Struct. Dyn. 17, 799-809 (2000) PDF
11. Berezovsky, I.N., Esipova, N.G. & Tumanyan, V.G.
Hierarchy of regions of amino acid sequence in aspect of their
role in the protein spatial structure.
J. Comp. Biol. 7, 183-192 (2000) PDF
2001
12. Berezovsky, I.N. & Trifonov, E.N.
Evolutionary aspects of protein structure and folding.
Mol. Biol. 35, 233-239 (2001) PDF
13. Berezovsky, I.N. & Trifonov, E.N.
Van der Waals locks: loop-n-lock structure of globular proteins.
J. Mol. Biol. 307, 1419-1426 (2001) PDF
14. Lamarine, M., Mornon, J.-P., Berezovsky I.N. & Chomilier, J.
Distribution of tightened end fragments of globular proteins statistically
match that of topohydrophobic positions: towards an efficient punctuation
of protein folding?
Cell. Mol. Life Sci. 58, 492-498 (2001) PDF
15. Berezovsky, I.N. & Trifonov, E.N.
Loop fold nature of globular proteins.
Protein Engineering 14, 403-407 (2001) PDF
16. Trifonov, E.N., Kirzhner, A., Kirzhner, V.M. & Berezovsky, I.N.
Distinct stages of protein evolution as suggested by protein sequence analysis.
J. Mol. Evol. 53, 394-401 (2001) PDF
17. Berezovsky, I.N., Kirzhner, A., Kirzhner, V.M. & Trifonov, E.N.
Protein folding: looping from the hydrophobic nuclei.
PROTEINS: Structure, Function, and Genetics 45, 346-350(2001)
PDF
18. Berezovsky, I.N. & Trifonov, E.N.
Protein structure and folding: a new start.
J. Biomol. Struct. & Dyn. 19, 397-403 (2001) PDF
19. Fain, A.V., Berezovskii, I.N., Tchehov, V.O., Ukrainskii, D.L. &
Esipova N.G.
Double and bifurkated bonds in alpha-helices of globular proteins.
Biophysics 46, 921-928 (2001) PDF1, PDF2, PDF3
2002
20. Trifonov, E.N. & Berezovsky, I.N.
Proteomic code.
Mol. Biol. 36, 239-243 (2002) PDF
21. Berezovsky, I.N.
Protein structure: chapters which have been missed.
In: Recent Research Developments
in Protein Folding, Stability and Design.
(Eds. M.M. Gromiha and S. Selvaraj) vol.1, pp.1-23
Transworld Research Network, Trivandrum, India (2002) PDF
22. Berezovsky, I.N. & Trifonov, E.N.
Loop fold structure of proteins: resolution of Levinthal's paradox.
J. Biomol. Struct. & Dyn. 20, 5-6 (2002) PDF
23. Trifonov, E.N. & Berezovsky, I.N.
Molecular evolution from abiotic scratch.
FEBS Letters 527, 1-4 (2002) PDF
24. Berezovsky, I.N. & Trifonov, E.N.
Back to units of protein folding.
J. Biomol. Struct. & Dyn. 20, 315-316 (2002) PDF
Link contains all Opinion Pieces on Levinthal paradox and protein folding
published in the issue
25. Berezovsky, I.N. & Trifonov, E.N.
Flowering buds of globular proteins: transpiring simplicity of protein organization.
Comparative and functional genomics 3, 525-534 (2002) PDF
26. Berezovsky, I.N., Kirzhner, V.M., Kirzhner, A., Rosenfeld V.R. & Trifonov, E.N.
Closed loops: persistence of the protein chain returns.
Protein Engineering 15, 955-957 (2002) PDF
2003
27. Berezovsky, I.N., Kirzhner, A., Kirzhner, V.M. & Trifonov, E.N.
An eye-opener to protein structure.
ComPlexUs 1, 29-37 (2003) PDF
28. Trifonov, E.N. & Berezovsky, I.N.
Evolutionary aspects of protein strcuture and folding.
Curr. Opin. Struct. Biol. 13, 110-114 (2003) PDF
29. Berezovsky, I.N.
Discrete structure of van der Waals domains in globular proteins.
Protein Engineering 16, 161-167 (2003) PDF
30. Berezovsky, I.N., Kirzhner, A., Kirzhner, V.M., Rosenfeld V.R. & Trifonov, E.N.
Protein sequnces yeild a proteomic code.
J. Biomol. Struct. & Dyn. 21, 317-325 (2003) PDF
31. Berezovsky, I.N., Kirzhner, A., Kirzhner, V.M. & Trifonov, E.N.
Spelling protein structure.
J. Biomol. Struct. & Dyn. 21, 327-339 (2003) PDF
32. Berezovsky, I.N. & Trifonov, E.N.
Protein structure: marriage with polymer statistics.
In: Protein Structures.
Kaleidoscope of Structural Properties and Functions.
(Ed. V.N. Uversky), vol.1, pp. 1-15.
Transworld Research Network, Trivandrum, India (2003) PDF
2004
33. Papandreou, N., Berezovsky, I.N., Lopes, A., Eliopoulos, E. & Chomilier, J.
Universal positions in globular proteins. From observation to simulation.
Eur. J. Biochem. 271, 4762-4768 (2004) PDF
2005
34. Berezovsky, I.N. & Shakhnovich, E.I.
Physics and evolution of thermophilic adaptation.
Proc. Nat. Acad. Sci. USA 102, 12742-12747 (2005) PDF
35. Berezovsky, I.N., Chen, W.W., Choi, P.J. & Shakhnovich, E.I.
Entropic stabilization of proteins and its proteomic consequences.
PLoS Comp. Biol. 102, e47 (2005).