Lecture

Computational Protein Design

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In course

BIOENG-320: Synthetic biology

This advanced Bachelor/Master level course will cover fundamentals and approaches at the interface of biology, chemistry, engineering and computer science for diverse fields of synthetic biology. This class requires critical and analytical thinking at the ...

Description

This lecture series on Synthetic Biology covers the journey from molecules to circuit to cell engineering, focusing on nucleic acid engineering, protein design, gene circuits, metabolic pathway engineering, protein circuits, and cell engineering. The instructor discusses the challenges in protein structure prediction and design, applications of computational protein design, and the importance of protein design in bioengineering and synthetic biology. The lecture also delves into the process of designing proteins, both experimentally and computationally, highlighting the significance of protein structures in determining protein function. Various topics such as the energy function for scoring the Global Minimum Energy Conformation (GMEC), atomic interactions in proteins, and the sampling methods for protein conformation exploration are explored.

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Instructors (3)

Vassily Hatzimanikatis

Dr. Vassily Hatzimanikatis is currently Associate Professor of Chemical Engineering and Bioengineering at Ecole Polytechnique Federale de Lausanne (EPFL), in Lausanne, Switzerland. Vassily received a PhD and an MS in Chemical Engineering from the California Institute of Technology, and his Diploma in Chemical Engineering from the University of Patras, in Greece. After the completion of his doctoral studies, he held a research group leader position at the Swiss Federal Institute of Technology in Zurich (ETHZ), Switzerland. Prior to joining EPFL, Vassily worked for three years in DuPont, Cargill, and Cargill Dow, and he has been assistant professor at Northwestern University, at Illinois, USA. Vassilys research interests are in the areas of computational systems biology, biotechnology, and complexity. He is associate editor of the journals Biotechnology & Bioengineering, Metabolic Engineering and Integrative Biology, and he serves on the editorial advisory board of the journals Bioprocess and Biosystems Engineering, Journal of Chemical Technology and Biotechnology, and Industrial Biotechnology. He has written over 70 technical publications and he is co-inventor in three patents and patent applications. Vassily is a fellow of the American Institute for Medical and Biological Engineering (2010), he was a DuPont Young Professor (2001-2004), and he has also received the Jay Bailey Young Investigator Award in Metabolic Engineering (2000), and the ACS Elmar Gaden Award (2011).

Patrick Daniel Barth

Professor Patrick Barth is Associate Professor at EPFL and Adjunct Associate Professor at Baylor College of Medicine, Houston, TX, USA. He received training in Physics, Chemistry and Biology (University of Paris, ENS) in France and performed his PhD at the Commissiariat a l'Energie Atomique in Saclay, France on structure/function studies of membrane proteins (photosystem I) using biochemical and biophysical experimental techniques. He carried out postdoctoral studies at University of California at Berkeley with Tom Alber on computational development for calculating protein electrostatics and designing de novo selective peptide inhibitors of cellular protein interactions. He then went to the University of Washington as a postdoctoral fellow and instructor in David Baker's laboratory to develop computational techniques in the software Rosetta for predicting and designing membrane protein structures. He started his independent career and received tenure at Baylor College of Medicine. He will continue at EPFL to marry computation and experiment for understanding the molecular determinants of signal transduction, as well as modeling and designing membrane proteins with novel functions for various synthetic biology and therapeutic applications.

Official source

Ontological neighbourhood

Chemistry

Biochemistry: Proteins

Related concepts (32)

Protein structure

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers - specifically polypeptides - formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond.

Protein folding

Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.

Protein

Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.

Protein tertiary structure

Protein tertiary structure is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure.

Protein structure prediction

Protein structure prediction is the inference of the three-dimensional structure of a protein from its amino acid sequence—that is, the prediction of its secondary and tertiary structure from primary structure. Structure prediction is different from the inverse problem of protein design. Protein structure prediction is one of the most important goals pursued by computational biology; and it is important in medicine (for example, in drug design) and biotechnology (for example, in the design of novel enzymes).

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