Lecture

Transmembrane Proteins: Hydrophobicity and Evolution

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In course

BIO-105: Cellular biology and biochemistry for engineers

Basic course in biochemistry as well as cellular and molecular biology for non-life science students enrolling at the Master or PhD thesis level from various engineering disciplines. It reviews essential notions necessary for a training in biology-related ...

Description

This lecture discusses the prediction of transmembrane domains in proteins using hydropathy plots, emphasizing the limitations of textbook examples. It also explores the relationship between the number of transmembrane domains and protein function, highlighting the evolutionary aspects of potassium channels and their classification into different families based on the number of transmembrane domains.

Instructor

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

Official source

Related concepts (28)

Transmembrane protein

A transmembrane protein (TP) is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents.

Protein

Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.

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.

Transmembrane domain

A transmembrane domain (TMD) is a membrane-spanning protein domain. TMDs may consist of one or several alpha-helices or a transmembrane beta barrel. Because the interior of the lipid bilayer is hydrophobic, the amino acid residues in TMDs are often hydrophobic, although proteins such as membrane pumps and ion channels can contain polar residues. TMDs vary greatly in size and hydrophobicity; they may adopt organelle-specific properties. Transmembrane domains are known to perform a variety of functions.

Evolution

In biology, evolution is the change in heritable characteristics of biological populations over successive generations. Evolution occurs when evolutionary processes such as natural selection (including sexual selection) and genetic drift act on genetic variation, resulting in certain characteristics becoming more or less common within a population over successive generations. The process of evolution has given rise to biodiversity at every level of biological organisation.

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