Lecture

Peptide Sequence Structure

Graph Chat

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

In course

MSE-212: Biology for engineers

Le cours est une introduction aux sciences de la vie en tant que domaine pluridisciplinaire ayant de multiples connexions avec l'ingénierie des matériaux. Il permettra aux étudiants de trouver dans la biologie une inspiration lors des leur activités dans l ...

Description

This lecture aims to teach the language of biologists to engineering students, focusing on writing peptide sequences correctly. The instructor explains the stereochemistry of amino acids, the chiral center, and the convention of representing peptide structures. By using a simple zigzag line method, students learn to fill in the amino acids' side groups, respecting stereochemistry to avoid mistakes. The lecture includes a practical exercise of writing down the peptide sequence EPFL, composed of glutamic acid, proline, phenylalanine, and lysine.

Instructors (2)

Romain Zufferey

Teaching & PhD Courses Biology for engineers MSE-212 This course consists of an introduction to biology and more particularly to biology as a multidisciplinary field, emphasizing natural examples of materials engineering. It should therefore allow engineering students to find inspiration from biology in future materials research problems. Cellular biology and biochemistry for engineers BIO-105 Basic course in biochemistry as well as cellular and molecular biology for non-life

Maartje Martina Cornelia Bastings

Expertise Can we use structural material properties on the nanoscale to engineer selective interactions at the bio-interface?The goal of the Programmable Biomaterials Lab is to understand the molecular design rules behind selective multivalent interactions at the bio-interface. We use DNA as engineering tool to explore the importance of structural mechanics and precise control of valency and patterns on directional interactions and self-assembly. Expertise Can we use structural material properties on the na

Official source

Related concepts (20)

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 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 quaternary structure

Protein quaternary structure is the fourth (and highest) classification level of protein structure. Protein quaternary structure refers to the structure of proteins which are themselves composed of two or more smaller protein chains (also referred to as subunits). Protein quaternary structure describes the number and arrangement of multiple folded protein subunits in a multi-subunit complex. It includes organizations from simple dimers to large homooligomers and complexes with defined or variable numbers of subunits.

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.

Protein primary structure

Protein primary structure is the linear sequence of amino acids in a peptide or protein. By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the laboratory. Protein primary structures can be directly sequenced, or inferred from DNA sequencess.

Related lectures (54)

Molecular Interactions in Biomolecules

Explores the energetic principles of molecular interactions in biomolecules, focusing on noncovalent interactions and the 3D structure of nucleic acids.

Proteins: Structure and Function

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

Protein Structure Exploration

Explores protein composition, synthesis, purification, and analysis techniques for understanding protein structure and function.

Protein Composition and Structure

Explores protein composition, peptide bonds, structures, folding, and stability.

Bio-material Transfer Strategies