Lecture

Protein Design: Structure and Function

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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 explores the fundamental concepts of protein design, focusing on the building blocks of protein structures, such as secondary structures and super secondary structures. It delves into the design of helices and beta sheets, the role of amino acids in secondary structure propensity, and the importance of loops in connecting different structural elements. The lecture also covers the definition of tertiary and quaternary structures, as well as the computational methods used in protein design, including Rosetta Design. Examples of protein design approaches and their applications in stabilizing proteins, designing new folds, and creating functional beta barrels are discussed.

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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.

Biomolecular structure

Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function. The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits. This useful distinction among scales is often expressed as a decomposition of molecular structure into four levels: primary, secondary, tertiary, and quaternary.

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.

Fusion protein

Fusion proteins or chimeric (kī-ˈmir-ik) proteins (literally, made of parts from different sources) are proteins created through the joining of two or more genes that originally coded for separate proteins. Translation of this fusion gene results in a single or multiple polypeptides with functional properties derived from each of the original proteins. Recombinant fusion proteins are created artificially by recombinant DNA technology for use in biological research or therapeutics.

Protein secondary structure

Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the protein folds into its three dimensional tertiary structure. Secondary structure is formally defined by the pattern of hydrogen bonds between the amino hydrogen and carboxyl oxygen atoms in the peptide backbone.

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