Proteins: Central Dogma and Translation

In course

Description

This lecture covers the process of protein synthesis, including transcription, translation, and the central dogma of molecular biology. It explains how mRNA is translated into proteins, the role of codons, and the importance of amino acids in protein folding.

Instructor

Official source

https://mediaspace.epfl.ch/media/0_mxugkt8f

About this result

This page is automatically generated and may contain information that is not correct, complete, up-to-date, or relevant to your search query. The same applies to every other page on this website. Please make sure to verify the information with EPFL's official sources.

Related lectures (322)

Related concepts (122)

Protein domain

In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions.

Ultrahydrophobicity

In chemistry and materials science, ultrahydrophobic (or superhydrophobic) surfaces are highly hydrophobic, i.e., extremely difficult to wet. The contact angles of a water droplet on an ultrahydrophobic material exceed 150°. This is also referred to as the lotus effect, after the superhydrophobic leaves of the lotus plant. A droplet striking these kinds of surfaces can fully rebound like an elastic ball. Interactions of bouncing drops can be further reduced using special superhydrophobic surfaces that promote symmetry breaking, pancake bouncing or waterbowl bouncing.

Hydrophobe

In chemistry, hydrophobicity is the physical property of a molecule that is seemingly repelled from a mass of water (known as a hydrophobe). In contrast, hydrophiles are attracted to water. Hydrophobic molecules tend to be nonpolar and, thus, prefer other neutral molecules and nonpolar solvents. Because water molecules are polar, hydrophobes do not dissolve well among them. Hydrophobic molecules in water often cluster together, forming micelles. Water on hydrophobic surfaces will exhibit a high contact angle.

Folding@home

Folding@home (FAH or F@h) is a distributed computing project aimed to help scientists develop new therapeutics for a variety of diseases by the means of simulating protein dynamics. This includes the process of protein folding and the movements of proteins, and is reliant on simulations run on volunteers' personal computers. Folding@home is currently based at the University of Pennsylvania and led by Greg Bowman, a former student of Vijay Pande.

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.