Protein Engineering
Enzymes represent by far the most advanced catalysts known to date and harnessing their catalytic potential is one of the major goals of biotechnology. Natural enzymes often need to be engineered before being used in industrial or pharmaceutical processes and directed evolution has emerged as a powerful tool to re-design enzyme by means of screening large libraries of mutants through iterative cycles of mutation and selection. Despite of the recent accomplishments of directed evolution protocols, the exhaustive exploration of the mutant space remains unattainable both experimentally and computationally. The proprietary Ulysses Protein Design™ platform integrates structural and computational data to identify those regions of the protein space with the higher density of functional mutants in order to streamline the protein engineering process and shorten experimental time.

ULYSSES Protein Design™: Smart Exploration of the Sequence Space for Enzyme and Protein Optimization

Our Ulysses in vitro selection system is a highly integrated platform capable to unlock the potential of in vitro selection procedure streamlining the entire process from the initial stage of DNA shuffling through cloning, selection and expression of improved mutants. The main features of our Ulysses in vitro selection platform are:

DirectRecombination - smart DNA shuffling
Our proprietary recombination method DirectRecombination allows the non-random recombination of DNA fragments when generating the initial recombinant DNA library. DNA recombination is a crucial step when searching the protein space for novel entities. To date, DNA recombination has been performed in several different ways most notably by DNA shuffling. DNA shuffling consists in the random assembling of DNA fragments derived from different sources. DNA shuffling has been successfully used in several works; however DNA shuffling, by means of random recombination of DNA fragments, neglects the evolutionary significance of DNA fragments and therefore reset to zero the informational content of a DNA sequence. As a consequence of random recombination, sequence space EXPLORAtion becomes less efficient due to the high rate of non-functional mutants. Conversely, our DirectRecombination method takes account of the evolutionary significance of DNA fragments during reassembling which results in a higher fraction of functional mutants. The straightforward consequence is a more efficient and fast EXPLORAtion of protein sequence space with an added value for our customers in terms of time and investment.

NetProt - identify protein hotspots with confidence
Proteins can be regarded as large and hyper-connected network of interacting residues, so that the effect of a given mutation propagates through the network and can affect even distance residues.  Our platform integrates structural and computational data to identify those regions of the protein space with the higher density of functional mutants in order to streamline the protein engineering process and shorten experimental time.

Fill-in the following form to contact us and discuss you project requirments

*mandatory fields
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	STEP1. Your Protein Data
Sample name *
Accession Number
Upload sequence
Master sequence (encoding gene)?	I'll will provide the master sequence in a ready-to-use vectorI'll will provide the master sequence as purified PCR product I request Explora to synthetise the encoding gene
Is you protein toxic to E.coli? *	No Yes I do not know
Is your protein a monomer? *	Yes it is a monomer No it is a dimer No it is a trimer No it is a multimer I do not know.
	STEP2. Optimise my protein to work at
Temperature [°C]:	e.g. 45°C
pH:	e.g. pH 4.7
Salt Concentration	e.g. NaCl 0.5M, MgCl2 0.125M, CuSO4‎ 0.250M
Detergent/Organic solvents/Chemicals:	e.g. CHAPS 1%, DTT 0.1M, Tween 20 20%
	STEP3. Your details
Full Name *
Your Institution *		Please provide us institution name, Country, Streeet, ZIP Code
Your Email
Your Phone		e.g 001-901-987654321
Enter code (dark letters)