Найдено научных статей и публикаций: 3, для научной тематики: Information structure of proteins
1.
Elena Svirshcevskaya, Ludmila Alekseeva, Alexei Marchenko, Sergei Benevolenski, Valentina M. Berzhec, Alexei Nekrasov
- Journal of Bioinformatics and Computational Biology , 2006
Sub-unit vaccines are synthetic or recombinant peptides representing T- or B-cell epitopes
of major protein antigens from a particular pathogen. Epitope selection requires
the synthesis of peptides that overlap the protein sequences and screening for the most
effective ones. In this study a new meth...
Sub-unit vaccines are synthetic or recombinant peptides representing T- or B-cell epitopes
of major protein antigens from a particular pathogen. Epitope selection requires
the synthesis of peptides that overlap the protein sequences and screening for the most
effective ones. In this study a new method of immunogenic peptide selection based on
the analysis of information structure of protein sequences is suggested. The analysis
of known B-cell epitope location in the information structure of Aspergillus fumigatus
proteins Asp f 2 and Asp f 3 has shown that epitopes are scattered along the sequences
of proteins for the exception of sites with Increased Degree Information Coordination
(IDIC). Based on these results peptides from different allergens such as Asp f 2, Der p 1,
and Fel d 1 were selected and produced in a recombinant form in the context of yeast virus-like particles (VLPs). Immunization of mice with VLPs containing peptides form
allergens has induced the production of IgG able to recognize full-length antigens. This
result suggests that the analysis of information structure of proteins can be used for the
selection of peptides possessing cryptic B-cell epitope activity.
Journal of Bioinformatics and Computational Biology
Vol. 4, No. 2, (2006), pp. 389–402.
2.
Alexei N. Nekrasov, Alexei A. Zinchenko
- Journal of Biomolecular Structure & Dynamics , 2008
The novel method allowing identification of protein structure elements responsible for catalytic
activity manifestation is proposed. Structural organization of various hydrolases was
studied using the ANIS (ANalysis of Informational Structure) method. ANIS allows to
reveal a hierarchy of the ELement...
The novel method allowing identification of protein structure elements responsible for catalytic
activity manifestation is proposed. Structural organization of various hydrolases was
studied using the ANIS (ANalysis of Informational Structure) method. ANIS allows to
reveal a hierarchy of the ELements of Information Structure (ELIS) using protein amino
acid sequence. The ELIS corresponds to the variable length sites with an increased density
of structural information. The amino acid residues forming the enzyme catalytic site were
shown to belong to the different top-ranking ELIS located in the contact area of the corresponding
spatial structure clusters. In the protein spatial structure catalytic sites are located
in the area of contact between fragments of polypeptide chain (structural blocs) allocation
to the different top-ranking ELIS. According to our results we concluded that structural
blocks corresponding to top-ranking ELIS are crucial for protein functioning. Such regions
are structurally independent, and their determinate mobility relative to each other is vital for
an efficient enzymatic reaction to occur.
Journal of Biomolecular Structure &
Dynamics, ISSN 0739-1102
Volume 25, Issue Number 5, (2008) pp. 553-561
3.
Alekseeva L., Nekrasov A., Marchenko A., Shevchenko M., Benevolenskii S., Sapozhnikov A., Kurup V.P., Svirshchevskaya E.
- Vaccine , 2007
A comparison of the location of B-cell epitopes and information structure (IS) of protein sequences was attempted. Analysis of 62 known
B-cell epitopes located in five different proteins showed that they concentrated in IS sites with increased degree of information coordination.
Based on the analy...
A comparison of the location of B-cell epitopes and information structure (IS) of protein sequences was attempted. Analysis of 62 known
B-cell epitopes located in five different proteins showed that they concentrated in IS sites with increased degree of information coordination.
Based on the analysis of IS six peptides from two proteins were selected and produced in a recombinant form as yeast virus-like particles
(VLPs). Immunization of mice with recombinant VLP-peptides has induced the production of IgG capable of recognizing full-length antigens.
This result suggests that the analysis of IS of proteins can be useful in the selection of peptides possessing cryptic B-cell epitope activity.
Vaccine 2007 vol. 25(14), pp. 2688-2697