Victor Vitoldovich Poboinev

RESEARCH INTERESTS

Molecular biology, proteomics, bioinformatics, biophysics, biochemistry, pathological physiology

Scopus Publications

Conjugation with the Carrier Helped to Reveal acidification-Induced Structural Shift in the Peptide from Phospholipase Domain of Parvovirus B19
Vladislav Victorovich Khrustalev, Olga Victorovna Khrustaleva, Aleksander Nicolaevich Stojarov, Anastasia Aleksandrovna Akunevich, Oleg Evgenyevich Baranov, Anna Vladimirovna Popinako, Elena Olegovna Samoilovich, Marina Anatolyevna Yermolovich, Galina Valeryevna Semeiko, Victoria Igorevna Cheprasova,et al.
Springer Science and Business Media LLC



A NEW APPROACH IN THE DEVELOPMENT OF A DENTAL CARIES VACCINE
S. P. Rubnikovich, V. V. Poboinev, and V. V. Khrustalev
Publishing House Belorusskaya Nauka
The genomes of the bacteria Streptococcus mutans and Streptococcus sobrinus, which cause dental caries, currently have been fully sequenced. However, the secondary and tertiary structures of the full-size surface proteins of these microorganisms, by which they attach to the surface of teeth covered with saliva, have not been instrumentally determined at the moment. There are a number of experimental studies on the use of these proteins in the process of developing a dental caries vaccine. However, there is currently no commercially available dental caries vaccine.The aim of the study was to choose an antigen for subsequent molecular modeling of a unique peptide for the development of a dental caries vaccine.To develop an effective and safe dental caries vaccine, it is necessary to perform a number of experiments in silico, preceding experiments in vitro and in vivo. Today, this approach is not only generally recognized, but also allows to significantly reduce the cost of experiments and time at the preclinical and clinical studies. According to our hypothesis, as an antigen for the development of a dental caries vaccine, it is necessary to use a short fragment of the surface protein (a peptide) of Streptococcus mutans and/or Streptococcus sobrinus, whose homology in amino acid sequence is 84.8  %, the spatial structure of which should correspond to the spatial structure of the corresponding fragment in a full-sized protein. In addition, the selected protein fragment, which will be part of the vaccine peptide, must be available to antibodies, i. e. located on the surface of the protein and defined as a B-cell linear and spatial epitope. Also, according to our hypothesis, the vaccine peptide may consist of the most stable fragments of alanine and proline rich regions of the surface protein of Streptococcus mutans and/or Streptococcus sobrinus for mutual stabilization of the spatial structure.


Structural Shifts of the Parvovirus B19 Capsid Receptor-binding Domain: A Peptide Study
Vladislav Victorovich Khrustalev, Aleksander Nicolaevich Stojarov, Anastasia Aleksandrovna Akunevich, Oleg Evgenyevich Baranov, Anna Vladimirovna Popinako, Elena Olegovna Samoilovich, Marina Anatolyevna Yermalovich, Galina Valeryevna Semeiko, Egor Gennadyevich Sapon, Victoria Igorevna Cheprasova,et al.
Bentham Science Publishers Ltd.
Background:: Binding appropriate cellular receptors is a crucial step of a lifecycle for any virus. Structure of receptor-binding domain for a viral surface protein has to be determined before the start of future drug design projects. Objective:: Investigation of pH-induced changes in the secondary structure for a capsid peptide with loss of function mutation can shed some light on the mechanism of entrance. Methods:: Spectroscopic methods were accompanied by electrophoresis, ultrafiltration, and computational biochemistry. Results:: In this study, we showed that a peptide from the receptor-binding domain of Parvovirus B19 VP1 capsid (residues 13-31) is beta-structural at pH=7.4 in 0.01 M phosphate buffer, but alpha- helical at pH=5.0, according to the circular dichroism (CD) spectroscopy results. Results of infra- red (IR) spectroscopy showed that the same peptide exists in both alpha-helical and beta-structural conformations in partial dehydration conditions both at pH=7.4 and pH=5.0. In contrast, the peptide with Y20W mutation, which is known to block the internalization of the virus, forms mostly alpha-helical conformation in partial dehydration conditions at pH=7.4. According to our hypothesis, an intermolecular antiparallel beta structure formed by the wild-type peptide in its tetramers at pH=7.4 is the prototype of the similar intermolecular antiparallel beta structure formed by the corresponding part of Parvovirus B19 receptor-binding domain with its cellular receptor (AXL). Conclusion:: Loss of function Y20W substitution in VP1 capsid protein prevents the shift into the beta-structural state by way of alpha helix stabilization and the decrease of its ability to turn into the disordered state.


Peptide Models of the Cytoplasmic Tail of Influenza A/H1N1 Virus Hemagglutinin Expand Understanding its pH-Dependent Modes of Interaction with Matrix Protein M1
Victor Vitoldovich Poboinev, Vladislav Victorovich Khrustalev, Anastasia Aleksandrovna Akunevich, Nikolai Vladimirovich Shalygo, Aleksander Nikolaevich Stojarov, Tatyana Aleksandrovna Khrustaleva, and Larisa Valentinovna Kordyukova
Springer Science and Business Media LLC



The PentUnFOLD algorithm as a tool to distinguish the dark and the light sides of the structural instability of proteins
Victor Vitoldovich Poboinev, Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, Tihon Evgenyevich Kasko, and Vadim Dmitrievich Popkov
Springer Science and Business Media LLC



Equilibrium Between Dimeric and Monomeric Forms of Human Epidermal Growth Factor is Shifted Towards Dimers in a Solution
Anastasia Aleksandrovna Akunevich, Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, Victor Vitoldovich Poboinev, Nikolai Vladimirovich Shalygo, Aleksander Nicolaevich Stojarov, Alexander Migranovich Arutyunyan, Larisa Valentinovna Kordyukova, and Yehor Gennadyevich Sapon
Springer Science and Business Media LLC
An interplay between monomeric and dimeric forms of human epidermal growth factor (EGF) affecting its interaction with EGF receptor (EGFR) is poorly understood. While EGF dimeric structure was resolved at pH 8.1, the possibility of EGF dimerization under physiological conditions is still unclear. This study aimed to describe the oligomeric state of EGF in a solution at physiological pH value. With centrifugal ultrafiltration followed by blue native gel electrophoresis, we showed that synthetic human EGF in a solution at a concentration of 0.1 mg/ml exists mainly in the dimeric form at pH 7.4 and temperature of 37 °C, although a small fraction of its monomers was also observed. Based on bioinformatics predictions, we introduced the D46G substitution to examine if EGF C-terminal part is directly involved in the intermolecular interface formation of the observed dimers. We found a reduced ability of the resulting EGF D46G dimers to dissociate at temperatures up to 50 °C. The D46G substitution also increased the intermolecular antiparallel β-structure content within the EGF peptide in a solution according to the CD spectra analysis that was confirmed by HATR-FTIR results. Additionally, the energy transfer between Tyr and Trp residues was detected by fluorescence spectroscopy for the EGF D46G mutant, but not for the native EGF. This allowed us to suggest the elongation and rearrangement of the intermolecular β-structure that leads to the observed stabilization of EGF D46G dimers. The results imply EGF dimerization under physiological pH value and temperature and the involvement of EGF C-terminal part in this process.


The cytoplasmic tail of influenza A/H1N1 virus hemagglutinin is β-structural
Vladislav V. Khrustalev, Larisa V. Kordyukova, Alexander M. Arutyunyan, Victor V. Poboinev, Tatyana A. Khrustaleva, Aleksander N. Stojarov, Lyudmila A. Baratova, Alena S. Sapon, and Valery G. Lugin
Informa UK Limited
Influenza A/H1N1 virus hemagglutinin (HA) is an integral type I glycoprotein that contains a large glycosylated ectodomain, a transmembrane domain, and a cytoplasmic tail (CT) of 10-14 amino acid residues. There are absolutely no data on the secondary or tertiary structure of the HA CT, which is important for virus pathogenesis. Three highly conserved cysteines are post-translationally modified by the attachment of fatty acid residues that pin the CT to the lipid membrane inside the virion. We applied circular dichroism (CD) and fluorescence spectroscopy analysis to examine four synthetic peptides corresponding to 14-15 C-terminal residues of H1 subtype HA (NH2-WMCSNGSLQCRICI-COOH; NH2-FWMCSNGSLQCRICI-COOH), with free or acetaminomethylated cysteines, in the reduced or non-reduced state, at various pH values and temperatures. The CD analysis detected the formation of a β-structure (30-65% according to the new BeStSel algorithm), in addition to an unstructured random coil, in every peptide in various conditions. It was completely or partially recognized as an antiparallel β-structure that was also confirmed by the multi-bounce Horizontal Attenuated Total Reflectance Fourier Transformed Infrared (HATR-FTIR) spectroscopy analysis. According to the experimental data, as well as 3 D modeling, we assume that the amino acid sequence corresponding to the HA CT may form a short antiparallel β-structure under the lipid membrane within a virion. Communicated by Ramaswamy H. Sarma.


Spectra of tryptophan fluorescence are the result of co-existence of certain most abundant stabilized excited state and certain most abundant destabilized excited state
Khrustalev Vladislav Victorovich, Khrustaleva Tatyana Aleksandrovna, Poboinev Victor Vitoldovich, Stojarov Aleksander Nicolaevich, Kordyukova Larisa Valentinovna, and Akunevich Anastasia Aleksandrovna
Elsevier BV
Fluorescence spectra of proteins and peptides are traditionally used to get an information on self-association of proteins and peptides, on their tertiary and quaternary structure. In this study it was shown that there are just three peaks of tryptophan fluorescence (at ∼308, at ∼330, and at ∼360 nm) in rough unsmoothed spectra of fluorescence of pure tryptophan in different solvents that change their heights depending on the polarity of a solvent. Two separate peaks at ∼330 nm and ∼360 nm are especially prominent in the spectrum of human epidermal growth factor. In contrast, in smoothed (either mathematically, or physically) spectra of Trp-containing proteins a single maximum of fluorescence varies between 330 and 360 nm. The theory of tryptophan fluorescence is discussed in light of three discrete peaks existence. A stabilizing hydrogen bond with aromatic system of benzene ring in the excited state is proposed as the cause of emission at ∼360 nm bringing Trp to the destabilized ground state. Emission from the destabilized excited state has a maximum at ∼330 nm if the ground state is destabilized, as well as if both states are stabilized. If the excited state is destabilized, while the ground state is stabilized by purely hydrophobic interactions, emitted light should have a maximum at ∼308 nm. The degree of hydrophilicity of tryptophan microenvironment is proposed to be measured as the ratio between the peak at 360 nm and the peak at 330 nm if the observed shifts are not "horizontal", but "vertical". The process of dissociation of hemagglutinin trimers from pandemic Influenza A(H1N1) virus is described as an example of the advantages of the proposed method.


Influence of mutations caused by radiation exposure on the bilirubin binding sites of human serum albumin
V. V. Poboinev, V. V. Khrustalev, A. N. Stojarov, and T. A. Khrustaleva
Publishing House Belorusskaya Nauka
In this article we analyze the bilirubin binding sites of human serum albumin from the point of view of the secondary structure instability, as well as the effect of amino acid substitutions caused by radiation exposure on the ability of albumin to bind bilirubin-IX-alpha. Based on calculations of binding energy and inhibition constants of bilirubin-albumin complexes before and after the amino acid substitutions, it was found that amino acid substitutions have different effects on the ability of human serum albumin to bind bilirubin. Amino acid substitutions Asp269-Gly269 (Nagasaki-1), Glu354-Lys354 (Hiroshima-1), Asp375-Asn375 (Nagasaki-2) reduce the binding free energy of bilirubin with human serum albumin, and the amino acid substitutions His3-Gln3 (Nagasaki-3) and Glu382-Lys382 (Hiroshima-2) increase it during molecular docking with the corresponding areas of the protein surface. The inhibition constants are significantly higher than with known binding sites. In general, mutations caused by radiation exposure cannot effect on bilirubin binding sites of human serum albumin, since the amino acid residues that are replaced do not interact with the amino acid residues from the binding sites (Leu115, Arg117, Phe134, Tyr138, Ile142, Phe149, Phe157, Tyr161, Arg186, Lys190, Lys240, Arg222). All amino acid residues from known binding sites are located in stable elements of the secondary structure of human serum albumin.The data obtained are important for understanding the impact of radiation exposure on the development of bilirubin encephalopathy in the population of the Chernobyl region and Japan.


Translation-Associated Mutational U-Pressure in the First ORF of SARS-CoV-2 and Other Coronaviruses
Vladislav Victorovich Khrustalev, Rajanish Giri, Tatyana Aleksandrovna Khrustaleva, Shivani Krishna Kapuganti, Aleksander Nicolaevich Stojarov, and Victor Vitoldovich Poboinev
Frontiers Media SA



Filamentous versus Spherical Morphology: A Case Study of the Recombinant A/WSN/33 (H1N1) Virus
Larisa V. Kordyukova, Ramil R. Mintaev, Artyom A. Rtishchev, Marina S. Kunda, Natalia N. Ryzhova, Sergei S. Abramchuk, Marina V. Serebryakova, Vladislav V. Khrustalev, Tatyana A. Khrustaleva, Victor V. Poboinev,et al.
Cambridge University Press (CUP)
AbstractInfluenza A virus is a serious human pathogen that assembles enveloped virions on the plasma membrane of the host cell. The pleiomorphic morphology of influenza A virus, represented by spherical, elongated, or filamentous particles, is important for the spread of the virus in nature. Using fixative protocols for sample preparation and negative staining electron microscopy, we found that the recombinant A/WSN/33 (H1N1) (rWSN) virus, a strain considered to be strictly spherical, may produce filamentous particles when amplified in the allantoic cavity of chicken embryos. In contrast, the laboratory WSN strain and the rWSN virus amplified in Madin–Darby canine kidney cells exhibited a spherical morphology. Next-generation sequencing (NGS) suggested a rare Ser126Cys substitution in the M1 protein of rWSN, which was confirmed by the mass spectrometric analysis. No structurally relevant substitutions were found by NGS in other proteins of rWSN. Bioinformatics algorithms predicted a neutral structural effect of the Ser126Cys mutation. The mrWSN_M1_126S virus generated after the introduction of the reverse Cys126Ser substitution exhibited a similar host-dependent partially filamentous phenotype. We hypothesize that a shortage of some as-yet-undefined cellular components involved in virion budding and membrane scission may result in the appearance of filamentous particles in the case of usually “nonfilamentous” virus strains.


Biochemical features of parvovirus B19 genovariant 1A2 dominating during the incidence rise in Belarus
M. A. Yermalovich, V. V. Khrustalev, T. A. Khrustaleva, V. V. Poboinev, and E. O. Samoilovich
Publishing House Belorusskaya Nauka
Two genovariants (1a1 and 1a2) are distinguished among Human parvovirus B19 (B19P) of subgenotype 1a, of which 1a2 was predominantly distributed during the incidence rise in Belarus. The aim of this study was a comparative analysis of the amino acid variability and of the mutational pressure directions in different parts of the genome between genovariants 1a1 and 1a2.The analysis of the consensus amino acid sequences of two genovariants and the three-dimensional structure models of protein fragments was carried out. In total, two unique amino acid substitutions in the main non-structural protein NS1 of 1a2 were found (I181M and E114G), one of which E114G is close to the DNA-binding domain (OBD) responsible for attachment to the replication origin site and can affect the rate of virus replication and transcription. Three unique amino acid substitutions were found in the structural polypeptide VP of 1a2: V30L, S98N, and N533S. Two of them are located in the most immunogenic region VP1u and can contribute to the escape from immune response. The investigation of the mutational pressure direction revealed a decrease in the frequency of G to T transversions in the second reading frame of 1a2, which reflects a higher transcription rate as a result of amino acid substitution in the OBD protein.The differences revealed between the genetic variants of subgenotype 1a B19P both in the antigenic sites and in the replication and transcription system can provide an increased “fitness” for the genetic variant 1a2 and explain its predominant distribution during the incidence rise.


Cobalt(ii) cation binding by proteins
Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, Victor Vitoldovich Poboinev, Carolina Igorevna Karchevskaya, Elizaveta Aleksandrovna Shablovskaya, and Tatyana Germanovna Terechova
Royal Society of Chemistry (RSC)
Herein, a set of non-homologous proteins (238) that could bind the cobalt(ii) cations was selected from all the available Protein Data Bank structures with Co2+ cations.


Microenvironment of tryptophan residues in proteins of four structural classes: applications for fluorescence and circular dichroism spectroscopy
Vladislav Victorovich Khrustalev, Victor Vitoldovich Poboinev, Aleksander Nicolaevich Stojarov, and Tatyana Aleksandrovna Khrustaleva
Springer Science and Business Media LLC



Mutational pressure and natural selection in epidermal growth factor receptor gene during germline and somatic mutagenesis in cancer cells
Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, Victor Vitoldovich Poboinev, and Konstantin Vyachislavovich Yurchenko
Elsevier BV



Amino acid content of beta strands and alpha helices depends on their flanking secondary structure elements
Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, and Victor Vitoldovich Poboinev
Elsevier BV



The part of a long beta hairpin from the scrapie form of the human prion protein is reconstructed in the synthetic CC36 protein
Vladislav Victorovich Khrustalev, Tatyana Aleksandrovna Khrustaleva, Kamil Szpotkowski, Victor Vitoldovich Poboinev, and Katsiaryna Yurieuna Kakhanouskaya
Wiley

RECENT SCHOLAR PUBLICATIONS

Conjugation with the Carrier Helped to Reveal acidification-Induced Structural Shift in the Peptide from Phospholipase Domain of Parvovirus B19
VV Khrustalev, OV Khrustaleva, AN Stojarov, AA Akunevich, OE Baranov, ...
The Protein Journal 43 (4), 805-818 2024



Новый подход к разработке вакцины от кариеса зубов
СП Рубникович, ВВ Побойнев, ВВ Хрусталёв
Известия Национальной академии наук Беларуси. Серия медицинских наук 21 (2 2024



Random coil to alpha helix structural shift in the peptide from phospholipase domain of Parvovirus B19 capsid conjugated with the carrier is caused by acidification of the medium
VV Khrustalev, OV Khrustaleva, AN Stojarov, AA Akunevich, OE Baranov, ...
2024



Structural shifts of the Parvovirus B19 capsid receptor-binding domain: a peptide study
VV Khrustalev, AN Stojarov, AA Akunevich, OE Baranov, AV Popinako, ...
Protein and Peptide Letters 31 (2), 128-140 2024



Молекулярная динамика белков термостабильных архей
МС Тарасик, ВВ Хрусталёв, ОВ Хрусталёва, ВВ Побойнев, ...
Минск: БГУ 2024



Peptide models of the cytoplasmic tail of influenza A/H1N1 virus hemagglutinin expand understanding its pH-dependent modes of interaction with matrix protein M1
VV Poboinev, VV Khrustalev, AA Akunevich, NV Shalygo, AN Stojarov, ...
The Protein Journal 42 (4), 288-304 2023



Выявление участков белков, склонных к определённым типам структурных переходов
ВВ Побойнев
БГМУ 2023



Оценка влияния аминокислотных замен на стабильность эпидермального фактора роста человека
ВА Козел, ВВ Побойнев
БГМУ 2023



Оценка студентами первого курса педиатрического факультета учебного процесса на кафедре общей химии учреждения образования Белорусский государственный медицинский университет
ВВ Побойнев, ВВ Хрусталёв, АР Козел, ТВ Латушко, ТВ Прохорова
БГМУ 2023



Лабораторные работы по медицинской химии
ВВ Хрусталёв, ОВ Хрусталёва, ТВ Латушко, ТВ Прохорова, ...
БГМУ 2023



The PentUnFOLD algorithm as a tool to distinguish the dark and the light sides of the structural instability of proteins
VV Poboinev, VV Khrustalev, TA Khrustaleva, TE Kasko, VD Popkov
Amino Acids 54 (8), 1155-1171 2022



The cytoplasmic tail of influenza A/H1N1 virus hemagglutinin is β-structural
VV Khrustalev, LV Kordyukova, AM Arutyunyan, VV Poboinev, ...
Journal of Biomolecular Structure and Dynamics 40 (10), 4642-4661 2022



Equilibrium between dimeric and monomeric forms of human epidermal growth factor is shifted towards dimers in a solution
AA Akunevich, VV Khrustalev, TA Khrustaleva, VV Poboinev, NV Shalygo, ...
The Protein Journal 41 (2), 245-259 2022



НАУЧНЫЙ И ОБРАЗОВАТЕЛЬНЫЙ ПРОЦЕСС НА КАФЕДРЕ ОБЩЕЙ ХИМИИ БГМУ В УСЛОВИЯХ ГЛОБАЛЬНЫХ ВЫЗОВОВ И ЦИФРОВИЗАЦИИ
ТВ Прохорова, ТВ Латушко, ВВ Побойнев, ВВ Хрусталёв
ББК 65.9 (4Беи), 108 2022



О ВЛИЯНИИ АМИНОКИСЛОТНОЙ ЗАМЕНЫ Y20W НА ВТОРИЧНУЮ СТРУКТУРУ ПЕПТИДА, СООТВЕТСТВУЮЩЕГО ФРАГМЕНТУ РЕЦЕПТОР-СВЯЗЫВАЮЩЕГО ДОМЕНА ПАРВОВИРУСА В19
ВВ Хрусталёв, ТА Хрусталёва, НВ Шалыго, АН Стожаров, ЕГ Сапон, ...
Молекулярные, мембранные и клеточные основы функционирования биосистем. К 2022



Инновационные технологии при изучении медицинской химии
ТВ Прохорова, ТВ Латушко, ВВ Побойнев
ББК 28.073 я431 С 23, 209 2022



Особенности койла, способного к структурному переходу в полностью неупорядоченное состояние
ВВ Побойнев, ВВ Хрусталёв
2022



СТРУКТУРНЫЕ ОСОБЕННОСТИ САЙТОВ СВЯЗЫВАНИЯ ХЛОРИД-ИОНОВ БЕЛКАМИ БАКТЕРИЙ С РАЗНОЙ GC-НАСЫЩЕННОСТЬЮ ГЕНОМОВ
ЮА Бондарь, ВВ Побойнев, ВВ Хрусталёв, ЕГ Ясевич
" БИОХИМИЯ XXI ВЕКА" 26 ноября 2021 года, 52 2021



Spectra of tryptophan fluorescence are the result of co-existence of certain most abundant stabilized excited state and certain most abundant destabilized excited state
KV Victorovich, KT Aleksandrovna, PV Vitoldovich, SA Nicolaevich, ...
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 257, 119784 2021



Analysis of helix-to-coil transitions in human serum albumin
V Paboineu, V Khrustalev, A Stazharau, T Khrustaleva
FEBS OPEN BIO 11, 172-172 2021

MOST CITED SCHOLAR PUBLICATIONS

Spectra of tryptophan fluorescence are the result of co-existence of certain most abundant stabilized excited state and certain most abundant destabilized excited state
KV Victorovich, KT Aleksandrovna, PV Vitoldovich, SA Nicolaevich, ...
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 257, 119784 2021
Citations: 24



Translation-associated mutational U-pressure in the first ORF of SARS-CoV-2 and other coronaviruses
VV Khrustalev, R Giri, TA Khrustaleva, SK Kapuganti, AN Stojarov, ...
Frontiers in Microbiology 11, 559165 2020
Citations: 21



Microenvironment of tryptophan residues in proteins of four structural classes: applications for fluorescence and circular dichroism spectroscopy
VV Khrustalev, VV Poboinev, AN Stojarov, TA Khrustaleva
European Biophysics Journal 48, 523-537 2019
Citations: 18



Amino acid content of beta strands and alpha helices depends on their flanking secondary structure elements
VV Khrustalev, TA Khrustaleva, VV Poboinev
Biosystems 168, 45-54 2018
Citations: 16



Cobalt(ii) cation binding by proteins
VV Khrustalev, TA Khrustaleva, VV Poboinev, CI Karchevskaya, ...
Metallomics 11 (10), 1743-1752 2019
Citations: 14



The part of a long beta hairpin from the scrapie form of the human prion protein is reconstructed in the synthetic CC36 protein
VV Khrustalev, TA Khrustaleva, K Szpotkowski, VV Poboinev, ...
Proteins: Structure, Function, and Bioinformatics 84 (10), 1462-1479 2016
Citations: 11



The PentUnFOLD algorithm as a tool to distinguish the dark and the light sides of the structural instability of proteins
VV Poboinev, VV Khrustalev, TA Khrustaleva, TE Kasko, VD Popkov
Amino Acids 54 (8), 1155-1171 2022
Citations: 10



The cytoplasmic tail of influenza A/H1N1 virus hemagglutinin is β-structural
VV Khrustalev, LV Kordyukova, AM Arutyunyan, VV Poboinev, ...
Journal of Biomolecular Structure and Dynamics 40 (10), 4642-4661 2022
Citations: 9



Mutational pressure and natural selection in epidermal growth factor receptor gene during germline and somatic mutagenesis in cancer cells
VV Khrustalev, TA Khrustaleva, VV Poboinev, KV Yurchenko
Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis 815, 1-9 2019
Citations: 7



Filamentous versus Spherical Morphology: A Case Study of the Recombinant A/WSN/33 (H1N1) Virus
LV Kordyukova, RR Mintaev, AA Rtishchev, MS Kunda, NN Ryzhova, ...
Microscopy and Microanalysis 26 (2), 297-309 2020
Citations: 4



Khrustalevа ТА Features of amino acid composition of beta-strands in proteins of different structural classes
VV Khrustalev, VV Poboinev
Fundamental’naya nauka v sovremennoi meditsine: materialy satellitnoi 2017
Citations: 4



Peptide models of the cytoplasmic tail of influenza A/H1N1 virus hemagglutinin expand understanding its pH-dependent modes of interaction with matrix protein M1
VV Poboinev, VV Khrustalev, AA Akunevich, NV Shalygo, AN Stojarov, ...
The Protein Journal 42 (4), 288-304 2023
Citations: 3



Stability of alpha-helical and beta-structural blocks in proteins of four structural classes
VV Poboinev, VV Khrustalev, TA Khrustaleva, AN Stozharov
Proceedings of the National Academy of Sciences of Belarus, Biological 2018
Citations: 3



Особенности аминокислотного состава альфа-спиральных участков в полипептидных цепях белков различных структурных классов
ВВ Побойнев, ВВ Хрусталев, ТА Хрусталева
Весці Нацыянальнай акадэміі навук Беларусі. Серыя біялагічных навук, 58-66 2017
Citations: 3



Особенности аминокислотного состава бета-тяжей в белках различных структурных классов
ВВ Хрусталёв, ВВ Побойнев, ТА Хрусталёва
Фундаментальная наука в современной медицине 2017, 331-336 2017
Citations: 3



Structural shifts of the Parvovirus B19 capsid receptor-binding domain: a peptide study
VV Khrustalev, AN Stojarov, AA Akunevich, OE Baranov, AV Popinako, ...
Protein and Peptide Letters 31 (2), 128-140 2024
Citations: 2



Equilibrium between dimeric and monomeric forms of human epidermal growth factor is shifted towards dimers in a solution
AA Akunevich, VV Khrustalev, TA Khrustaleva, VV Poboinev, NV Shalygo, ...
The Protein Journal 41 (2), 245-259 2022
Citations: 2



Инновационные технологии при изучении медицинской химии
ТВ Прохорова, ТВ Латушко, ВВ Побойнев
ББК 28.073 я431 С 23, 209 2022
Citations: 2



Стабильность альфа-спиральных и бета-структурных блоков в белках четырех структурных классов
ВВ Побойнев, ВВ Хрусталёв, ТА Хрусталёва, АН Стожаров
Известия Национальной академии наук Беларуси. Серия биологических наук 63 (4 2018
Citations: 2



Khrustaleva ТА Features of amino acid composition of alpha-helical regions in proteins of different structural classes
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