The correlations were performed on real solutions in a biochemical laboratory.
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Selection of flexible antibody chains to antigen, determination of affinity, change in entropy, dissociation energy for each modification of the antibody. -modification of antibody flexible chains, -stepwise testing of each antibody to antigen, -determination of key amino acid residues, -range of changes in affinity.
Molecular Profiling of Tumors: The Future of Personalized Medicine. Analysis of the biochemical reaction scheme taking into account the characteristics of each patient's disease, since the concept of "oncological disease" is a complex disease, the obtained results will then be sorted into certain groups according to the characteristics obtained.
Calculation of the influence of ions and ATP molecules on the physical properties of proteins, monomers, dimers, tetramers. Study of small inhibitors, calculation of atomic charges, comparison of the obtained results, construction of comparative graphs so that the experimenter could see a preliminary possible experimental results
Protein+Inhibitor+Atom
AI Prices for Inhibitors Calculations
The influence of small inhibitors on protein interactions
Price list /Main categories of molecular complexes with small inhibitors or atoms, and a list of prices for calculating each molecular complex.
Features
Set one
Set two
Set Three
Set Four
[Monomer+Inhibitor] or Atom
up to 10 mutations
up to 40 mutations
up to 150 mutations
up to 250 mutations [3-4weeks]
up to TWO inhibitors
[Dimer+Inhib.1+Inhib.2] or Atoms
up to 30 mutations
up to 100 mutations
up to 150 mutations [3-5 weeks]
up to 4 inhibitors
[Tetramer+Several Inh-s] [Trimer+Several Inhib-s]
up to 10 mutations
up to 50 mutations [6-8 weeks]
[pentamer+Several Inh-s] [any protein complex +Inh.]
up to 10 mutations
50 Euro
130 Euro
249 Euro
349 Euro
Linear models for finding correlations
We present the developed algorithm for a step-by-step transparent and understandable search for interaction areas, each of which will be characterized by numerical physical quantities. Use the linear docking method developed by us, which allows us to determine the most stable binding regions according to the amino acid sequence.
We propose to carry out the check with entire domains, i.e. to divide the molecule into structural elements, to determine the most contact amino acid sequences by the method of linear docking.
The interaction between sites will be characterized by numerical indicators, which will allow for a visual gradation.
Load a simple letter sequence of two protein sequences, while trying to ensure that the length of the proteins is a multiple of the length of the specified shift frame. The results will be automatically sent to your e-mail.
1. Application of optimization problems allows you to reconstruct the RNA structure. 2. The server produces a set of data indicating the stability of each section of RNA.
AI Prices for Linea Docking Calculations.
Calculations of Temperature Effect
Indication of the number of the amino acid residue that will be phosphorylated, from one to three amino acid residues.
The influence of solvent characteristics and experimental conditions on the nature of biochemical reactions.
If you need to calculate the aggregation of amyloid proteins/ peptides under various experimental conditions, you can use our software or perform the calculation online on the server and get clear and understandable preliminary results taking into account various experimental conditions.
1. Application of optimization problems allows you to reconstruct the RNA structure. 2. The server produces a set of data indicating the stability of each section of RNA.
Correlation analysis between experimental and calculated data for salt solutions revealed an acceleration in achieving agreement between experimental and calculated data. Therefore, it is advisable to carry out the calculation at low concentrations of salt in the solution 0.1mM-10mM
The maximum correlation dependence between the calculated and experimental values ​ was found between lg(cond(W)) and [Urea]50 in solution. Starting with C[Urea] >=2.8M and more. The correlation dependence between the values ​​​​reached 90%
Molecular 3D structure calculations
Start calculate Effects of Single Mutations on Protein Stability (Aggregation) right now! We offer to study an individual peptide only for 2.49 Euro, using AI and machine learning methods. Obtain a complete set of physical interaction parameters rpteoins
Load a simple letter sequence of two protein sequences, while trying to ensure that the length of the proteins is a multiple of the length of the specified shift frame. The results will be automatically sent to your e-mail.
We present the developed algorithm for a step-by-step transparent and understandable search for interaction areas, each of which will be characterized by numerical physical quantities. Use the linear docking method developed by us, which allows us to determine the most stable binding regions according to the amino acid sequence.
Individual study of the effect of mutations on complex formation, taking into account complex structures: dimers, tetramers, pentamers, taking into account the influence of additional structures: small inhibitors, allosteric inhibition, binding to DNA and RNA
Individual study of the effect of mutations on complex formation, taking into account complex structures: dimers, tetramers, pentamers, taking into account the influence of additional structures: small inhibitors, allosteric inhibition, binding to DNA and RNA
Perform alanine scanning of a large size monomeric protein with sequential replacement of amino acid residues in the polypeptide chain with alanine and obtain a set of changes in physical characteristics compared to the wild-type monomer.
Alaning scaning/Mutagenesis of large size monomeric/dimer protein
The length of the protein polypeptide chain is up to 1300 a.a.
Price:
Number of Substitutions in one protein:
up 30 Mutations
up 50 Mutations
up 100 Mutations
Perform alanine/Missence mutations scanning for dimer with sequential replacement of amino acid residues in one polypeptide chain and obtain a set of changes in physical characteristics compared to the wild-type monomer.
Perform an alanine scan of the polypeptide chain with known 3D structures Trimers/Tetramers
Price:
Duration:
about Month
about 6 -8 weeks
about 8-10 weeks
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Quantum problems, search for correlation laws, statistics, machine learning methods
Our team is engaged in fundamental research, so we will be glad to cooperate and your question via the feedback form!