His primary areas of investigation include Crystallography, Stereochemistry, Protein structure, Biochemistry and Transmembrane domain. His work carried out in the field of Crystallography brings together such families of science as Bacteriorhodopsin, Two-dimensional nuclear magnetic resonance spectroscopy, Hydrogen bond and Micelle. His Nuclear magnetic resonance spectroscopy and Nuclear Overhauser effect study, which is part of a larger body of work in Stereochemistry, is frequently linked to Side chain and Lantibiotics, bridging the gap between disciplines.
In Protein structure, Alexander S. Arseniev works on issues like Peptide, which are connected to Trypsin inhibitor and Protein purification. His research on Biochemistry frequently connects to adjacent areas such as Biophysics. His Transmembrane domain study incorporates themes from Transmembrane protein, Peptide sequence and Signal transduction, Receptor tyrosine kinase.
His main research concerns Biophysics, Stereochemistry, Crystallography, Biochemistry and Transmembrane domain. His research integrates issues of Receptor, Ligand, Cell membrane, Lipid bilayer and Binding site in his study of Biophysics. His work in the fields of Stereochemistry, such as Nuclear magnetic resonance spectroscopy, overlaps with other areas such as Side chain.
His Crystallography research includes elements of Bacteriorhodopsin, Membrane, Relaxation and Micelle. The concepts of his Transmembrane domain study are interwoven with issues in Transmembrane protein, Dimer, Receptor tyrosine kinase, Signal transduction and Membrane protein. His Protein structure research integrates issues from Vesicle and Circular dichroism.
His primary scientific interests are in Biophysics, Transmembrane domain, Nuclear magnetic resonance spectroscopy, Receptor and Cell biology. His work deals with themes such as Micelle, Transmembrane protein, Protein structure, Lipid bilayer and Membrane protein, which intersect with Biophysics. His Transmembrane protein study integrates concerns from other disciplines, such as Receptor tyrosine kinase and Ligand.
His research integrates issues of Cleavage, Signal transduction, Neurotrophin and Enzyme in his study of Transmembrane domain. His Nuclear magnetic resonance spectroscopy study combines topics in areas such as Sodium nitrite, Membrane, Phospholipid, Protein secondary structure and Binding site. His research investigates the connection with Stereochemistry and areas like Structural motif which intersect with concerns in Peptide.
The scientist’s investigation covers issues in Biophysics, Transmembrane domain, Protein structure, Structural motif and Ion channel. His Biophysics study incorporates themes from POPC and Lipid bilayer. His Lipid bilayer research incorporates themes from Bound water, Nuclear magnetic resonance spectroscopy and Micelle, Aqueous solution.
The various areas that Alexander S. Arseniev examines in his Transmembrane domain study include Cleavage, Receptor tyrosine kinase, Signal transduction and Transmembrane protein. His Structural motif research focuses on subjects like Potassium channel blocker, which are linked to Peptide. Alexander S. Arseniev has researched Ion channel in several fields, including Neurotoxin, Arginine, Venom and Stereochemistry.
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Three-dimensional structure of ectatomin from Ectatomma tuberculatum ant venom.
Dmitry E. Nolde;Alexander G. Sobol;Kirill A. Pluzhnikov;Eugene V. Grishin.
Journal of Biomolecular NMR (1995)
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.
Journal of Biological Chemistry (2008)
Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death trigger.
Eduard V. Bocharov;Yulia E. Pustovalova;Konstantin V. Pavlov;Pavel E. Volynsky.
Journal of Biological Chemistry (2007)
Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy.
Vladislav Yu. Orekhov;Konstantine V. Pervushin;Alexander S. Arseniev.
FEBS Journal (1994)
Conformation and mode of membrane interaction in cyclotides. Spatial structure of kalata B1 bound to a dodecylphosphocholine micelle.
Zakhar O. Shenkarev;Kirill D. Nadezhdin;Vladimir A. Sobol;Alexander G. Sobol.
FEBS Journal (2006)
NMR solution spatial structure of ‘short’ scorpion insectotoxin I5A
Alexander S. Arseniev;Vladimir I. Kondakov;Vladimir N. Maiorov;Vladimir F. Bystrov.
FEBS Letters (1984)
Molecular lipophilicity in protein modeling and drug design
Roman G. Efremov;Anton O. Chugunov;Timothy V. Pyrkov;John P. Priestle.
Current Medicinal Chemistry (2007)
Spatial Structure of the Transmembrane Domain Heterodimer of ErbB1 and ErbB2 Receptor Tyrosine Kinases
Konstantin S. Mineev;Eduard V. Bocharov;Yulia E. Pustovalova;Olga V. Bocharova.
Journal of Molecular Biology (2010)
The Chemical Basis of Fungal Bioluminescence
Konstantin V. Purtov;Valentin N. Petushkov;Mikhail S. Baranov;Konstantin S. Mineev.
Angewandte Chemie (2015)
Lipid-protein nanodiscs for cell-free production of integral membrane proteins in a soluble and folded state: comparison with detergent micelles, bicelles and liposomes.
E.N. Lyukmanova;Z.O. Shenkarev;N.F. Khabibullina;N.F. Khabibullina;G.S. Kopeina;G.S. Kopeina.
Biochimica et Biophysica Acta (2012)
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