R
Roman G. Efremov
Researcher at Russian Academy of Sciences
Publications - 225
Citations - 4684
Roman G. Efremov is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: Lipid bilayer & Transmembrane protein. The author has an hindex of 38, co-authored 205 publications receiving 4068 citations. Previous affiliations of Roman G. Efremov include Moscow Institute of Physics and Technology & Moscow State University.
Papers
More filters
Journal ArticleDOI
Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state.
Eduard V. Bocharov,Konstantin S. Mineev,Pavel E. Volynsky,Yaroslav S. Ermolyuk,Elena N. Tkach,A.G. Sobol,Vladimir Chupin,Kirpichnikov Mp,Roman G. Efremov,Alexander S. Arseniev +9 more
TL;DR: The spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 embedded into lipid bicelles was obtained by solution NMR, followed by molecular dynamics relaxation in an explicit lipid bilayer, providing an explanation for the pathogenic power of some oncogenic mutations.
Journal ArticleDOI
PLATINUM: a web tool for analysis of hydrophobic/hydrophilic organization of biomolecular complexes.
TL;DR: The PLATINUM web service is designed for analysis and visualization of hydrophobic/hydrophilic properties of biomolecules supplied as 3D-structures and provides a number of tools for quantitative characterization of the hydrophilic match in biomolecular complexes.
Journal ArticleDOI
Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death trigger.
Eduard V. Bocharov,Yulia Pustovalova,Konstantin V. Pavlov,Pavel E. Volynsky,Marina V. Goncharuk,Yaroslav S. Ermolyuk,Dmitry V. Karpunin,Alexey A. Schulga,Kirpichnikov Mp,Roman G. Efremov,Innokenty V. Maslennikov,Alexander S. Arseniev +11 more
TL;DR: The right-handed parallel helix-helix structure of the transmembrane domain with a hydrogen bond-rich His-Ser node in the middle of the membrane, accessibility of the node for water, and continuous hydrophilic track across the membrane suggest that the domain can provide an ion-conducting pathway through the membrane.
Journal ArticleDOI
Molecular lipophilicity in protein modeling and drug design
Roman G. Efremov,Anton O. Chugunov,Timothy V. Pyrkov,John P. Priestle,Alexander S. Arseniev,Edgar Jacoby +5 more
TL;DR: It is demonstrated that the application of the MHP-based techniques in combination with other molecular modeling tools permits significant improvement to the standard computational approaches, provides additional important insights into the intimate molecular mechanisms driving protein assembling in water and in biological membranes, and helps in the computer-aided drug discovery process.
Journal ArticleDOI
Surface‐enhanced Raman spectroscopy of biomolecules. Part I.—water‐soluble proteins, dipeptides and amino acids
TL;DR: In this paper, the surface-enhanced Raman spectra of water-soluble proteins (lysozyme and bovine serum albumin), dipeptides and amino acids were analysed.