Rasa Bioinformatic CRO Lab offer high quality protein tertiary structures custom modeling services based on your own amino-acid sequences. Combination of modeling and short term simulations under controlled parameters will ensure the reliability of modeled structure for further studies RASA’s protein modeling service comprise of integration of several highly recommended approaches ranging from homology, ab-initio or threading. We can customize and perform modeling as per client. Rasa Bioinformatic Lab are proud to say that we can very successfully model the complex of the proteins.
One of the important parts of research in structural biology is to generate a protein structure form the genetic data or the gene.At RASA Bioinformatic Lab, our experts understand the nuances of this and are extremely capable of converting your genetic data into a protein structure using the information provided by the client or curating that information. Our team can successfully translate the genetic sequence into a protein sequence which our experts can then successfully convert into protein structure. Rasa Contract Reaserch Orgnaisation can build protein models using minimal information such as: FASTA sequence, Sequence ID or Protein name.
The term “homology modeling“, also called comparative modeling or sometimes template-based modelling (TBM), refers to modeling a protein 3D structure using a known experimental structure of a homologous protein (the template). We at RASA follow a comparative modelling routine needing three items of input: The sequence of the protein with unknown 3D structure, the “target sequence“, a 3D template is chosen by virtue of having the highest sequence identity with the target sequence. Structural information is always of great assistance in the study of protein function, dynamics, interactions with ligands and other proteins. The “low-resolution” structure provided by homology modeling contains sufficient information about the spatial arrangement of important residues in the protein and may guide the design of new experiments, for example site-directed mutagenesis. Even within the pharmaceutical industry homology modeling can be valuable in structure-based drug discovery and drug design.
The ab initio prediction methods consist in modelling all the energetic involved in the process of folding, and then in finding the structure with lowest free energy. This approach is based on the ‘thermodynamic hypothesis’, which states that the native structure of a protein is the one for which the free energy achieves the global minimum. While ab initio prediction is clearly the most difficult, it is arguably the most useful approach. There are two components to ab initio prediction: devising a scoring (ie, energy) function that can distinguish between correct (native or native-like) structures from incorrect ones, and a search method to explore the conformational space. In many methods, the two components are coupled together such that a search function drives, and is driven by, the scoring function to find native-like structures.
Threading is also known as Fold Recognition, with this method, you can predict the protein structures of your target protein using known protein folds of similar proteins found in different databases. Online web servers, such as I-Tasser, Phyre2 and others give an insight on working of threading method.
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Apart from the package of services provided by us, we also customize service for our clients.
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RASA experts help you to model 3D protein structures & identify opportunities to streamline your research with genomics & proteomic data analysis.
RASA experts help you to manage, organize,analyze your any type of genomic data by using gold standard Next generation sequencing data analysis i.e NGS Data Analysis methods.
RASA prowess in computational chemistry, structural biology, molecular modelling, simulation.
We at RASA understand that the research you do is innovative and novel. Innovative research needs innovative solutions.We do provide customization in our services according to your research requirement.