Mediaspace scheduled maintenance: Aug 25, 2026 07:00 - 12:00 AM. During this time, videos will be temporarily unavailable. Check status updates.

Lecture

Transmembrane Beta Sheets

In course

BIO-207: Cellular and molecular biology II

This course is aimed to familiarize students with the 3D organization of a eukaryotic cell, its compartmentalization, how cellular compartments communicate together and how a cell communicates with its environment. The related molecular mechanisms will be ...

Description

This lecture covers the structure of transmembrane beta sheets, including the formation of parallel and antiparallel strands, the importance of side chains in hydrophobicity, and examples of transmembrane beta sheets in proteins like porins and perforin. The instructor explains how these structures are crucial for the function of certain proteins in both bacteria and animals.

Instructors (3)

Françoise Gisou van der Goot Grunberg

Gisou van der Goot is the Head of the Laboratory of Cell and Membrane Biology, and founding member of the Global Health Institute (GHI), School of Life Sciences, at the Swiss Federal Institute of Technology Lausanne/EPFL (Ecole Polytechnique Fédérale de Lausanne). She is currently Vice President for Responsible Transformation, in charge of reinforcing values such as inclusion and sustainability throughout the School’s campus. From 2014 to 2020, she was Dean of the School of Life Sciences. Before joining EPFL, she was Group Leader at the Faculty of Sciences of the University of Geneva (UNIGE) and subsequently Associate Professor at the Faculty of Medicine of the same university. She studied engineering at the Ecole Centrale de Paris, then did a PhD in Molecular Biophysics at the Nuclear Energy Research Center, Saclay, France, followed by a postdoc at the European Molecular Biology Laboratory (EMBL) in Heidelberg. She obtained an EMBO Young Investigator award in 2001, a Howard Hughes International Scholar award in 2005 and the Swiss Prix Marcel Benoist in 2009, the same year she was elected EMBO member (European Molecular Biology Organisation). She is a leader in the fields of molecular and cellular understanding of bacterial toxins, the organization of mammalian membranes and in organelles biology. Professor van der Goot is member of diverse scientific boards such as the Swiss National Science Foundation (SNF), the Conseil suisse de la science et de la technologie (CSST) and the European Research Council (ERC).

Wouter Richard Karthaus

Romain Zufferey

Official source

Related concepts (16)

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 (32)

Protein Composition and Structure

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

Protein Structure: General Principles

Discusses the organization of protein structures and the role of protein folding.

Protein Interaction Fingerprinting with Geometric Deep Learning

Explores deciphering protein interaction fingerprints using geometric deep learning and the challenges in computational protein-protein interaction design.

Proteins: Structure and Function

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