Lecture

Protein Design: Synthetic Biology

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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 covers the principles of protein design in synthetic biology, focusing on the common building blocks of protein structure, such as secondary structures, helices, beta sheets, loops, and super secondary structures. It also discusses the challenges in designing stable membrane proteins, the importance of protein stability, and the computational approaches used in protein design. The instructor presents examples of protein design for stability and functionality, including the design of a new fold and the optimization of protein structures through computational methods.

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Instructors (3)

Yimon Aye

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.

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Related concepts (31)

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.

Nucleic acid secondary structure

Nucleic acid secondary structure is the basepairing interactions within a single nucleic acid polymer or between two polymers. It can be represented as a list of bases which are paired in a nucleic acid molecule. The secondary structures of biological DNAs and RNAs tend to be different: biological DNA mostly exists as fully base paired double helices, while biological RNA is single stranded and often forms complex and intricate base-pairing interactions due to its increased ability to form hydrogen bonds stemming from the extra hydroxyl group in the ribose sugar.

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.

Integral membrane protein

An integral, or intrinsic, membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All transmembrane proteins are IMPs, but not all IMPs are transmembrane proteins. IMPs comprise a significant fraction of the proteins encoded in an organism's genome. Proteins that cross the membrane are surrounded by annular lipids, which are defined as lipids that are in direct contact with a membrane protein.

Peripheral membrane protein

Peripheral membrane proteins, or extrinsic membrane proteins, are membrane proteins that adhere only temporarily to the biological membrane with which they are associated. These proteins attach to integral membrane proteins, or penetrate the peripheral regions of the lipid bilayer. The regulatory protein subunits of many ion channels and transmembrane receptors, for example, may be defined as peripheral membrane proteins.

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