Protein Design: Synthetic Biology

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.

About this result

This page is automatically generated and may contain information that is not correct, complete, up-to-date, or relevant to your search query. The same applies to every other page on this website. Please make sure to verify the information with EPFL's official sources.

Related lectures (40)

Related concepts (39)

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

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.

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.

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 structure prediction

Nucleic acid structure prediction is a computational method to determine secondary and tertiary nucleic acid structure from its sequence. Secondary structure can be predicted from one or several nucleic acid sequences. Tertiary structure can be predicted from the sequence, or by comparative modeling (when the structure of a homologous sequence is known).

Protein Design: Structure and Function BIOENG-320: Synthetic biology

Covers protein design fundamentals, including secondary structures, amino acid propensity, loops, and computational methods.

Protein Folding: Structure and Design

Explores protein folding, hydrophobic interactions, compact conformations, the HP model, co-evolution, and computational methods.

Proteins: Structure and Function BIO-105: Cellular biology and biochemistry for engineers

Explores the structure and function of proteins, emphasizing their diverse roles in living organisms.

Protein Composition and Structure CH-210: Biochemistry

Explores protein composition, peptide bonds, secondary structures, and protein folding prediction.

Plasma Membrane Structure and Proteins BIO-105: Cellular biology and biochemistry for engineers

Covers plasma membrane structure, protein composition, fatty acid variations, protein folding, and amino acid properties.