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PROTEIN ENGG MEET 2020

4th International Conference on Protein Engineering 2020

Helsinki, Finland
13 - 14 July 2020
The conference ended on 14 July 2020

Important Dates

Abstract Submission Deadline
30th June 2020
Early Bird Deadline
30th June 2020

About PROTEIN ENGG MEET 2020

Protein engineering is the longest running independent life science events with a predominantly academic client base. It is important to note that while this conference focuses on Protein, Genetic, and Enzyme Engineering, Structure and Function of Proteins, Genomics & Structural Genomics, Protein Engineered Biomaterials, Proteomics in Plant & Animal, Pharmacogenomics & Pharmacoproteomics, Mass Spectrometry in Proteome Research, Transcriptome analysis & Gene Expression, Protein Biochemistry, Antibody Drug Therapy, Protein Therapeutics & Market Analysis, Molecular Modelling and Drug Designing, Bioinformatics and Computational Biology, Applications of Genetic and Protein Engineering, Machine Learning Applications in Bioinformatics and other techniques.

Call for Papers

Protein engineering is the process of developing useful or valuable proteins. It is a young discipline, with much research taking place into the understanding of protein folding and recognition for protein design principles.

There are two general strategies for protein engineering: rational protein design and directed evolution. These methods are not mutually exclusive; researchers will often apply both. In the future, more detailed knowledge of protein structure and function, and advances in high-throughput screening, may greatly expand the abilities of protein engineering. Eventually, even unnatural amino acids may be included, via newer methods, such as expanded genetic code, that allow encoding novel amino acids in genetic code.

Rational protein design approaches make protein-sequence predictions that will fold to specific structures. These predicted sequences can then be validated experimentally through methods such as peptide synthesis, site-directed mutagenesis, or artificial gene synthesis.

Rational protein design dates back to the mid-1970s. Recently, however, there were numerous examples of successful rational design of water-soluble and even trans membrane peptides and proteins, in part due to a better understanding of different factors contributing to protein structure stability and development of better computational methods.

  Directed evolution (DE) is a method used in protein engineering that mimics the process of natural selection to steer proteins or nucleic acids toward a user-defined goal. It consists of subjecting a gene to iterative rounds of mutagenesis (creating a library of variants), selection (expressing those variants and isolating members with the desired function) and amplification (generating a template for the next round). It can be performed in vivo (in living organisms), or in vitro (in cells or free in solution). Directed evolution is used both for protein engineering as an alternative to rationally designing modified proteins, as well as studies of fundamental evolutionary principles in a controlled, laboratory environment.

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