Prof. Alexei Finkelstein
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow, Russia
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Academic Career Length
57Years (1970-Present)
(Calculated once Scilit publication data is synced: current year − year of first publication + 1)
Representative Publications
View All Publications18 August 2004 in Proteins: Structure, Function, and Bioinformatics
Journal Article
EKElmar Krieger
Elmar KriegerTDTom Darden
Tom Darden
SNSander B. Nabuurs
Sander B. Nabuurs
Alexei FinkelsteinGVGert Vriend
Gert Vriend
1 September 2003 in Protein Science
Journal Article
DIDmitry N. Ivankov
Dmitry N. IvankovSGSergiy O. Garbuzynskiy
Sergiy O. GarbuzynskiyEAEric Alm
Eric Alm
KPKevin Plaxco
Kevin PlaxcoDBDavid Baker
David BakerAlexei FinkelsteinGuided by the recent success of empirical model predicting the folding rates of small two‐state folding proteins from the relative contact order (CO) of their native structures, by a theoretical model of protein folding that predicts that logarithm of the folding rate decreases with the protein chain length L as L2/3, and by the finding that the folding rates of multistate folding proteins strongly correlate with their sizes and have very bad correlation with CO, we reexamined the dependence of folding rate on CO and L in attempt to find a structural parameter that determines folding rates for the totality of proteins. We show that the Abs_CO = CO × L, is able to predict rather accurately folding rates for both two‐state and multistate folding proteins, as well as short peptides, and that this Abs_CO scales with the protein chain length as L0.70 ± 0.07 for the totality of studied single‐domain proteins and peptides.
1 April 1998 in Folding and Design
Journal Article
28 September 1999 in Proceedings of the National Academy of Sciences
Journal Article
OGOxana V. Galzitskaya
Oxana V. Galzitskaya
Alexei FinkelsteinWhen a protein folds or unfolds, it has to pass through many half-folded microstates. Only a few of them can be seen experimentally. In a two-state transition proceeding with no accumulation of metastable intermediates [Fersht, A. R. (1995)Curr. Opin. Struct. Biol.5, 79–84], only the semifolded microstates corresponding to the transition state can be outlined; they influence the folding/unfolding kinetics. Our aim is to calculate them, provided the three-dimensional protein structure is given. The presented approach follows from the capillarity theory of protein folding and unfolding [Wolynes, P. G. (1997)Proc. Natl. Acad. Sci. USA94, 6170–6175]. The approach is based on a search for free-energy saddle point(s) on a network of protein unfolding pathways. Under some approximations, this search is rapidly performed by dynamic programming and, despite its relative simplicity, gives a good correlation with experiment. The computed folding nuclei look like ensembles of those compact and closely packed parts of the three-dimensional native folds that contain a small number of disordered protruding loops. Their estimated free energy is consistent with the rapid (within seconds) folding and unfolding of small proteins at the point of thermodynamic equilibrium between the native fold and the coil.
1 January 1989 in Protein Engineering, Design and Selection
Journal Article
Alexei FinkelsteinJJJoël Janin
Joël Janin
1 October 1989 in Biopolymers
Journal Article
ESEvgeny I. Shakhnovich
Evgeny I. Shakhnovich
Alexei FinkelsteinAbout Me
Alexei V. Finkelstein, born June 16, 1947, graduated with honors from the Moscow Phys.-Tech. (1970), and later earned his PhD from the Moscow Phys.-Tech. (1976) and DSc from the Moscow Lomonosov University (1991).
Since 1970, he has been with the Institute of Protein Research (Russian Academy of Sciences), Protein Physics Laboratory (then headed by Prof. O.B. Ptitsyn). Now he heads this laboratory (since 1999). He is currently a Professor at the Moscow Lomonosov University (since 1998), and a Soros Professor (2001).
He is the author of >300 papers, and has written a book titled "Protein Physics", which is published in Russian (6 editions), English (2 editions), and Chinese (2 editions), as well as another book titled "Physics of Protein Molecules" (available in Russian).
Citation index: >12000, Hirsch index: 52.
Expertise: Molecular and protein physics; protein structures, folding, and design; structural transitions in proteins and amyloids; antifreeze proteins and ice nucleators; phase transitions; the Mpemba effect; force fields; molecular biology; and bioinformatics.
He has received awards from FIRCA, INTAS, CASP, HHMI (3 times), NWO, RSF, etc., as well as the State Prize of Russia in Science & Technology (1999). He has been elected to the Russian Academy of Sciences (2008).