D
Dmitry N. Ivankov
Researcher at Skolkovo Institute of Science and Technology
Publications - 51
Citations - 2017
Dmitry N. Ivankov is an academic researcher from Skolkovo Institute of Science and Technology. The author has contributed to research in topics: Protein folding & Folding (chemistry). The author has an hindex of 18, co-authored 43 publications receiving 1591 citations. Previous affiliations of Dmitry N. Ivankov include Pompeu Fabra University & Institute of Science and Technology Austria.
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Journal ArticleDOI
Local fitness landscape of the green fluorescent protein.
Karen S. Sarkisyan,Dmitry A. Bolotin,Margarita Meer,Dinara R. Usmanova,Dinara R. Usmanova,Alexander S. Mishin,George V. Sharonov,Dmitry N. Ivankov,Dmitry N. Ivankov,Nina G. Bozhanova,Mikhail S. Baranov,Onuralp Soylemez,Natalya S. Bogatyreva,Natalya S. Bogatyreva,Peter K. Vlasov,Evgeny S. Egorov,Maria D. Logacheva,Maria D. Logacheva,Maria D. Logacheva,Alexey S. Kondrashov,Alexey S. Kondrashov,Dmitry M. Chudakov,Ekaterina V. Putintseva,Ilgar Z. Mamedov,Dan S. Tawfik,Konstantin A. Lukyanov,Fyodor A. Kondrashov,Fyodor A. Kondrashov +27 more
TL;DR: An extensive region of the local fitness landscape of the green fluorescent protein from Aequorea victoria (avGFP) is visualize by measuring the native function (fluorescence) of tens of thousands of derivative genotypes of avGFP, indicating congruence between the fitness landscape properties at the local and global scales.
Journal ArticleDOI
Contact order revisited: Influence of protein size on the folding rate
Dmitry N. Ivankov,Sergiy O. Garbuzynskiy,Eric J. Alm,Kevin W. Plaxco,David Baker,Alexei V. Finkelstein +5 more
TL;DR: It is shown 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 thisAbs_CO scales with the protein chain length as L0.70 ± 0.07 for the totality of studied single‐domain proteins and peptides.
Journal ArticleDOI
Prediction of protein folding rates from the amino acid sequence-predicted secondary structure.
TL;DR: A method for predicting folding rates of proteins from their amino acid sequences only, or rather, from their chain lengths and their helicity predicted from their sequences is presented.
Journal ArticleDOI
Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics.
TL;DR: It is demonstrated that chain length is the main determinant of the folding rate for proteins with the three‐state folding kinetics and the logarithm of their folding rate in water strongly anticorrelates with their chain length L.
Journal ArticleDOI
Folding nuclei in proteins
TL;DR: The aim is to review recent experimental and theoretical studies of the folding nuclei and outline the transition state (‘folding nucleus’) by its key influence on the folding–unfolding kinetics.