Lecture

Microsecond Time-Resolved Cryo-EM: Bonus

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In course

CH-310: Dynamics and kinetics

The course covers the principles of chemical kinetics, including differential rate laws, derivation of exact and approximate integral rate laws for common elementary and composite reactions, fundamentals of collision and transition state theories, and appl ...

Description

This lecture delves into the development of a new approach for high-speed observations of proteins, focusing on large-amplitude domain motions, fast backbone motions, side chain motions, catalysis, protein folding, substrate binding, and allosteric regulation. It explores time-resolved methods offering atomic resolution, cryo-electron microscopy, in-situ melting and revitrification, real-time observation of rapid melting, and proof of principle experiments. The lecture also covers temperature control, capsid dynamics of CCMV, and future outlooks in the field of cryo-EM imaging.

Instructor

Ulrich Lorenz

Teaching & PhD PhD Students Jakub Hruby Past EPFL PhD Students Pavel Olshin, Gabriele Bongiovanni, Chengcheng Yan, Oliver Florian Harder, Mowry Nathan Junior, Constantin Richard Krüger

Official source

Ontological neighbourhood

Chemistry

Biochemistry: Proteins

Related concepts (31)

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.

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.

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