Published in International Journal of Molecular Sciences
This review focuses on the molecular signatures of protein structures in relation to evolution and survival in global warming. It is based on the premise that the power of evolutionary selection may lead to thermotolerant organisms that will repopulate the planet and continue life in general, but perhaps with different kinds of flora and fauna. Our...
Published in International Journal of Molecular Sciences
Protein cysteines often play crucial functional and structural roles, so they are emerging targets to design covalent thiol ligands that are able to modulate enzyme or protein functions. Some of these residues, especially those involved in enzyme mechanisms—including nucleophilic and reductive catalysis and thiol-disulfide exchange—display unusual ...
Published in Biomeditsinskaia khimiia
Izuchenie vzaimodeĭstviia poverkhnostnykh virusnykh belkov s model'nymi fosfolipidami vazhno dlia podrobnogo issledovaniia mekhanizmov proniknoveniia virusov v kletki pri infitsirovanii. Podkhodiashcheĭ sistemoĭ, modeliruiushcheĭ kletochnuiu membranu, iavliaiutsia liposomy. Metodom ravnovesnoĭ adsorbtsii issledovali sviazyvanie gemaggliutinina (NA)...
Published in Pure and Applied Chemistry
Adsorption is one of the most widely used processes in physicochemical operations. To design an adsorbent for a specific adsorbate, it is important to understand the interactions between adsorbents and adsorbates, which are very important for both adsorption capacity and selectivity. Electrostatic interactions, hydrogen bonding, hydrophobic interac...
Published in Molecular pharmaceutics
Amyloidosis is a well-known but poorly understood phenomenon caused by the aggregation of proteins, often leading to pathological conditions. For example, the aggregation of insulin poses significant challenges during the preparation of pharmaceutical insulin formulations commonly used to treat diabetic patients. Therefore, it is essential to devel...
Published in Journal of biomolecular structure & dynamics
Minidumbbell (MDB) is a newly found non-B DNA structure formed by short single-strand sequences. Up to now, three MDBs have been reported to form at neutral pH by sequences containing two repeats of TTTA, CCTG and CTTG. Among them, the thermodynamically less stable TTTA and CCTG MDBs have been proposed to be the structural intermediates that cause ...
Published in Russian Journal of Physical Chemistry A
AbstractInteraction of anionic surfactant, sodium dodecyl sulfate (SDS) with antibiotic drug cefradine monohydrate (CFD) were carried out in H2O/low concentration urea medium through conductivity measurement. The variation of critical micelle concentration (CMC) of SDS with the addition of drug (CFD) discloses the presence of interaction between SD...
Published in Chemistry (Weinheim an der Bergstrasse, Germany)
Polar groups have a solvent ordering effect on water and therefore may affect hydrophobic binding energies for nearby lipophilic surfaces. This would mean that determinations of excess surface free energy association energies require consideration of nearby polar functional groups. This paper reports results of a study to measure this possible effe...
Published in Bioinformatics and Biology Insights
The tetratricopeptide repeat (TPR) of proteins consists of a 34-amino acid, alpha-helical motif that comprises a pattern of small and large hydrophobic residues, leading to a recognizable signature sequence. Structural and functional studies have documented that tandem TPRs form a superhelix that interacts with client molecules through strategicall...
Published in Russian Journal of Physical Chemistry A
AbstractBy conductivity method were examined the aggregation behavior of cationic amphiphile–cetyltrimethylammonium bromide (CTAB) and anionic amphiphile–sodium dodecyl sulfate (SDS) mixtures in binary mixtures of various salts. The values of critical micelle concentration (cmc) of SDS–CTAB mixtures lie between the cmc values of the pure amphiphile...
