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Lecture

Proteins and Hydrophobicity

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 and folding of proteins, focusing on transmembrane proteins and the importance of hydrophobicity. It explains the role of amino acids, both polar and non-polar, in protein structure, and discusses the folding process of soluble and membrane proteins.

Instructors (3)

Wouter Richard Karthaus

Romain Zufferey

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).

Official source

Related concepts (17)

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.

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.

Essential amino acid

An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized from scratch by the organism fast enough to supply its demand, and must therefore come from the diet. Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are valine, isoleucine, leucine, methionine, phenylalanine, tryptophan, threonine, histidine, and lysine.

Protein fold class

In molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple, independent protein superfamilies (i.e. are not necessarily evolutionarily related to one another). Four large classes of protein that are generally agreed upon by the two main structure classification databases (SCOP and CATH).

Proteinogenic amino acid

Proteinogenic amino acids are amino acids that are incorporated biosynthetically into proteins during translation. The word "proteinogenic" means "protein creating". Throughout known life, there are 22 genetically encoded (proteinogenic) amino acids, 20 in the standard genetic code and an additional 2 (selenocysteine and pyrrolysine) that can be incorporated by special translation mechanisms.

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