Design of stable circular permutants of the GroEL chaperone apical domain.

Autor: Melnik TN; Institute of Protein Research, Russian Academy of Sciences, Institutskaja Str. 4, Pushchino, Moscow Region, 142290, Russia., Majorina MA; Institute of Protein Research, Russian Academy of Sciences, Institutskaja Str. 4, Pushchino, Moscow Region, 142290, Russia., Vorobeva DE; Institute of Protein Research, Russian Academy of Sciences, Institutskaja Str. 4, Pushchino, Moscow Region, 142290, Russia., Nagibina GS; Institute of Protein Research, Russian Academy of Sciences, Institutskaja Str. 4, Pushchino, Moscow Region, 142290, Russia., Veselova VR; Institute of Protein Research, Russian Academy of Sciences, Institutskaja Str. 4, Pushchino, Moscow Region, 142290, Russia., Glukhova KA; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Institutskaja Str. 3, Puschino, Moscow Region, 142290, Russia., Pak MA; Center for Molecular and Cellular Biology, Skolkovo Institute of Science and Technology, Bolshoy Boulevard 30, Bld. 1, Moscow, 121205, Russia., Ivankov DN; Center for Molecular and Cellular Biology, Skolkovo Institute of Science and Technology, Bolshoy Boulevard 30, Bld. 1, Moscow, 121205, Russia., Uversky VN; Department of Molecular Medicine and USF Health Byrd Alzheimer's Center and Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, USA. vuversky@usf.edu.; Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia. vuversky@usf.edu., Melnik BS; Institute of Protein Research, Russian Academy of Sciences, Institutskaja Str. 4, Pushchino, Moscow Region, 142290, Russia. bmelnik@phys.protres.ru.; Pushchino Branch, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Prospekt Nauki 6, Pushchino, Moscow Region, 142290, Russia. bmelnik@phys.protres.ru.

Publikováno v: Cell communication and signaling : CCS [Cell Commun Signal] 2024 Feb 01; Vol. 22 (1), pp. 90. Date of Electronic Publication: 2024 Feb 01.

Design and Analysis of a Mutant form of the Ice-Binding Protein from Choristoneura fumiferana.

Autor: Deeva AA; Biophysics Department, Siberian Federal University, Svobodny 79, Krasnoyarsk, Russia, 660041., Glukhova KA; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Puschino, Russia., Isoyan LS; Biophysics Department, Siberian Federal University, Svobodny 79, Krasnoyarsk, Russia, 660041., Okulova YD; Institute of Protein Research of the Russian Academy of Sciences, 4 Institutskaya Str., Pushchino, Moscow Region, Russia, 142290., Uversky VN; Department of Molecular Medicine and Byrd Alzheimer's Research Institure, Morsani College of Medicine, University of South Florida, Tampa, FL, USA., Melnik BS; Institute of Protein Research of the Russian Academy of Sciences, 4 Institutskaya Str., Pushchino, Moscow Region, Russia, 142290. bmelnik@phys.protres.ru.

Publikováno v: The protein journal [Protein J] 2022 Apr; Vol. 41 (2), pp. 304-314. Date of Electronic Publication: 2022 Apr 02.

Verification of the Stabilized Protein Design Based on the Prediction of Intrinsically Disordered Regions: Ribosomal Proteins L1.

Autor: Nagibina GS; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. galina-nagibina@phys.protres.ru., Marchenkov VV; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia., Glukhova KA; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia., Melnik TN; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia., Melnik BS; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.

Publikováno v: Biochemistry. Biokhimiia [Biochemistry (Mosc)] 2020 Jan; Vol. 85 (1), pp. 90-98.

Intrinsic Disorder-Based Design of Stable Globular Proteins.

Autor: Nagibina GS; Institute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Moscow Region, Russia., Glukhova KA; Institute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Moscow Region, Russia., Uversky VN; Department of Molecular Medicine and Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.; Institute for Biological Instrumentation of the Russian Academy of Sciences, Federal Research Center 'Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences', Pushchino 142290, Moscow Region, Russia., Melnik TN; Institute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Moscow Region, Russia., Melnik BS; Institute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Moscow Region, Russia.

Publikováno v: Biomolecules [Biomolecules] 2019 Dec 30; Vol. 10 (1). Date of Electronic Publication: 2019 Dec 30.

[Artificial Cysteine Bridges on the Surface of Green Fluorescent Protein Affect Hydration of Its Transition and Intermediate States].

Autor: Melnik TN; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.; tmelnik@vega.protres.ru., Nagibina GS; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia., Surin AK; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia., Glukhova KA; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia., Melnik BS; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.

Publikováno v: Molekuliarnaia biologiia [Mol Biol (Mosk)] 2018 Jan-Feb; Vol. 52 (1), pp. 88-97.