Biological and medical physics

Introductory video on the practical use of our software
To study the whole variety of physical characteristics of protein complexes, it is necessary to combine a large number of different experimental approaches, each of which allows one to determine only a narrow list of the required physical parameters, due to their limitations. Thus, using our software package you can determine the range of changes in affinity and then select only those modifications for further experimental research that meet the set objectives, for example, antibody modifications that will increase the affinity to the antigen, but will not lead to aggregation of antibodies among themselves.
Description of the software package for determining the stability of protein molecules.
UP TITLE
Thanks to the use of the software developed by us, you can determine the affinity of the biological complex before carry out the biological experiment.
Binomial Soft will allow you to determine the range of variation of the experimental values in biological research.
The purpose of our software development is to determine the affinity of a biological complex, which is comparable to such experimental values as Kd (a specific type of equilibrium constant), EC50 (half maximal effective concentration), ΔH, potential energy of interaction.

Moreover, we want to share our method with other people how to use methods by other laboratories around the world, as this will significantly accelerate the development of drugs against other diseases. Take the development of targeted drugs to a new level in the field of exact biochemistry.

You can contact us and reduce a lot of fail experiments for searching new molecules

Below are some biological research areas to which our software package can be applied.

TUTORIAL BIOLOGICAL SOFT. The figures show two graphs showing the results of the effect of mutations in the BAK peptide on binding to the Bcl-xl protein. The graph on the left is from an experimental study.
The figure shows a tetramer consisting of two CD20 transmembrane proteins and two FABs, heavy and light chains We will introduce five mutations in turn into the active binding site with CD20 and analyze the change in stability.


Our research can be divided into fundamental (basic) and applied biological researches.

Molecular biophysics is the study of the physical principles governing biomolecular systems. It seeks to explain biological function in terms of molecular structure, dynamics and organization, from single molecules to supramolecular structures.
Now let's analyze, and then perform example of replacing an amino acid residue in a Bak peptide when it interacts with the whole protein Bcl xl, which leads to an increase in the affinity of the peptide to the protein. Let us consider in more detail the three-dimensional structure of this dimer. Initially, we have a 3D structure of a dimer, in which the Q77L substitution in the Bak peptide is performed. The overall structure of BAKQ77L was not significantly affected by the mutation, and the side chain of L77 is oriented identically to the wild-type glutamine at this position on the solvent-exposed surface of the (BH3) helix.
Example 2: guide to biological software

Antibody Affinity

Biophysics of the affinity of the antibody-antigen biocomplex
Our group developed an innovative method in biology for antibody-antigen development. You don't have to spend money to carry out the experiment.
The correct determination of antibody affinity is crucial for antibody development as a wrong setup of the experiments may result in the further development of the wrong candidate antibody. This can result in low in vivo efficacy, especially when high-affinity antibodies are needed, for example, for neutralizing antibodies.
Our group has developed an innovative research technique for such a complex using Data Science
Learn More
Coronavirus (Covid-19) is a world pandemic. A step-by-step guide to the analysis of affinity of interaction by Soft using
This article describe a detailed method for selecting inhibitors based on modified natural peptides for the SARS-CoV protein spike glycoprotein. The selection of inhibitors is carried out by increasing the affinity of the peptide to the active center of the protein. The article also provides a step-by-step guide to the analysis of affinity of interaction by comparing 3 criteria, presents an analysis of energy interactions between the active center of a protein and the wild-type peptide interacting with it and taking into account modifications of the latter.
Learn More
New Approaches for Aggregation Mechanisms in Amyloids
We concluded that the dimers of mutant amyloids form stable and unstable dimeric complexes. If the dimeric complex is stable, then the formation of high molecular weight structures was much slower. This was due to the fact that the stable amyloid peptides were in no hurry to enter into chemical reactions with other amyloid peptides to achieve equilibrium.
It remained to solve the question: how will we determine the stability of the dimeric complex
Learn More
DATABASE OF TARGETED ANTITUMOR THERAPY FOR EGFR PROTEINS: HER2 AND HER3. Soft application.
Our method is molecularly selective, targeting certain oncogenic molecules, namely the EGFR family of tyrosine kinases, which occupy a significant share in the causes of oncogenic diseases. The diagram shows the percentage of mutations in proteins of the EGFR family in non-small cell lung cancer. Most people have relatives or friends who are sick or who have already left us. In 2017, 9.6 million people are estimated to have died from the various forms of cancer. Every sixth death in the world is due to cancer, making it the second leading cause of death — second only to cardiovascular diseases.
Learn More
What is hydrophobic interaction?
The most common explanation is that hydrophobic molecules "do not like" to interact with the aqueous environment. We obtained the values of hydrophobic interactions, calculated their value, developed a method for determining the range of interactions, and developed a graphical representation using soft, math, data science. You can free download soft and learn Data Scince
hydrophobic interactions
hydrophobic interaction, bio-molecules, protein-protein interactions, peptide, innovation
What researches are you interested in?
Here you can ask a question, talk about the goals of your research.
E-mail
You can leave a comment by choosing several options or send your message
Message
Or you can choose the most suits for you
Choose the right option
Additional information

Protein-protein interactions. Miscellaneous.

Examples of various calculations taking into account three-dimensional structure, as well as without taking into account three-dimensional structure

Fundamental (basic) research

Mathematical [math] methods, soft, data science and their physical application

Advance techniques and Physical Applications provides a wide range of basic math concepts and methods, which are relevant to biophysic theory and biomolecule. This page is devoted to the physical and mathematical modeling of the formation of complexes of protein molecules, antibody and amyloid peptide (alzheimer desease). Real techniques show remarkable sensitivity to the amino acid sequences of proteins, which facilitates experimental studies in lab and allows one to reduce the associated costs by reducing the number of measurements required according to the developed criteria in experimental lab. These models make it possible to reach a conclusion about the interactions between different amino acid chains and to identify more stable sites on proteins via control techniques, soft and Data Science. The models also take the phosphorylation of amino acid residues into account.
You can free download soft for antibody cost saving and learn Data Scince
Didn't find what you were looking for? Perhaps you still have questions. You can leave your question on an interesting topic of research. Our experts will answer you shortly
E-mail
Name
Comments

Behind the big data

Sign up to our newsletter

Get a selection of useful weekly articles
Made on
Tilda