Lecture

Protein 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

BIOENG-110: General Biology

Le but du cours est de fournir un aperçu général de la biologie des cellules et des organismes. Nous en discuterons dans le contexte de la vie des cellules et des organismes, en mettant l'accent sur les principes de réglementation que vous rencontrerez dan ...

Description

This lecture covers the primary, secondary, tertiary, and quaternary structures of proteins, detailing the sequence of amino acids, local folding, long-range folding, and large-scale assemblies. It also explains the interactions between amino acid side chains, the formation of alpha helices and beta sheets, and the role of different amino acids in protein structures.

Instructors (5)

Kristina Schoonjans

Expertise Bile acid signalingNutrient sensingIntermediary metabolismMetabolic disorders Teaching & PhD PhD Students Adrien Faure Past EPFL PhD Students Pan Xu, Ece Yildiz, Nadia Bresciani, Yu Sun, Francesca Pontanari, Alejandro Alonso Calleja Past EPFL PhD Students as codirector Mitsunori Nomura, Pan Xu, Katyayanee Neopane, Lucie Camille Chanvillard, Jakob Josef Langer, Bilge Sen Elçi Courses General Biology BIOENG-110 The purpose of the course is to provide a general overview of the biolo

Johannes Gräff

Academic appointments 2013- Tenure Track Assistant Professor, Swiss Federal Institute of Technology (EPFL), Lausanne, Switzerland, School of Life Sciences, Brain Mind Institute. 2009-2013 Postdoctoral fellow, Massachusetts Institute of Technology (MIT), Cambridge, USA, Picower Institute for Learning and Memory. 2009 Postdoctoral associate, Swiss Federal Institute of Technology (ETHZ), Zürich, Switzerland, Brain Research Institute. Education 2009 PhD in Neurosciences, Swiss Federal Institute of Technology (ETHZ), Zürich, Switzerland, Department of Biology, Brain Research Institute. 2005 Diploma (M.Sc. equivalent) in Biological Sciences, University of Lausanne, Switzerland, Faculty of Biology and Medicine, Department of Ecology and Evolution. 1998 Matura, Gymnasium Type B, Kantonsschule am Burggraben St. Gallen, Switzerland.

Camille Véronique Bernadette Goemans

Camille's research focuses on understanding how antibiotics and non-antibiotic drugs affect the diverse bacteria from the human gut microbiota and how they contribute to dysbiosis and the development of antibiotic resistance. To achieve this goal, she combines systems approaches with molecular microbiology, bacterial genetics and biochemistry.She obtained her Bachelor's and Master's degrees in Biomedical Sciences from the UCLouvain, Belgium, after which she completed her PhD (FRIA national fellowship) at th

Freddy Radtke

Freddy Radtke obtained his Ph.D. in Molecular Biology from the University of Zürich in 1994. In 1995, he started his postdoctoral research in the laboratory of Michel Aguet at Genentech, Inc. (San Francisco, USA). In 1997, he returned to Switzerland with Michel Aguet and finished his postdoctoral fellowship at the Swiss Institute for Experimental Cancer Research (ISREC) in Lausanne. From 1999‑2005, he was a group leader and Associate Member at the Ludwig Institute for Cancer Research. Freddy Radtke then joined ISREC in January 2006 as a senior scientist and in July 2006, he was appointed Associate Professor at the EPFL School of Life Sciences

Official source

Ontological neighbourhood

Chemistry

Biochemistry: Proteins

Related concepts (29)

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.

Amino acid

Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the α-amino acids, from which proteins are composed. Only 22 α-amino acids appear in the genetic code of all life. Amino acids can be classified according to the locations of the core structural functional groups, as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, ionization, and side chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.

Nucleic acid structure

Nucleic acid structure refers to the structure of nucleic acids such as DNA and RNA. Chemically speaking, DNA and RNA are very similar. Nucleic acid structure is often divided into four different levels: primary, secondary, tertiary, and quaternary. Nucleic acid sequence Primary structure consists of a linear sequence of nucleotides that are linked together by phosphodiester bond. It is this linear sequence of nucleotides that make up the primary structure of DNA or RNA.

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.

Related lectures (32)

Molecular Interactions in Biomolecules

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

Hydropathy Scales and Amino Acids Interaction

Explores hydropathy scales for amino acids and their role in predicting protein structure and function.

Peptide Sequence Structure

Teaches how to write peptide sequences correctly using a simple zigzag line method and emphasizes the importance of respecting stereochemistry to avoid mistakes.

Protein Analysis: Physico-Chemical Properties Determination

Covers experimental and computational methods for analyzing protein physico-chemical properties.

Proteins: Structure, Function, and Interactions