Mediaspace scheduled maintenance: Aug 25, 2026 07:00 - 12:00 AM. During this time, videos will be temporarily unavailable. Check status updates.

Lecture

Protein Folding: Structure and Interactions

In course

PHYS-441: Statistical physics of biomacromolecules

Biological macromolecules such as DNA, RNA, proteins and cytoskeletal filaments are polymers. As such, they share a set of properties that are common to any polymer, which are the focus of this course. Details about the protein folding problem will be cove ...

Description

This lecture delves into the intricate process of protein folding, exploring the formation of chemical bonds between amino acids and the emergence of polypeptide chains. The instructor discusses the translation of RNA messages into specific proteins at the ribosome, emphasizing the importance of the native state conformation. The lecture also covers the role of attractive forces in protein collapse and the unique compact conformations accessible. Various amino acids, their chemical properties, and the significance of their side chains in protein folding are explained. The lecture concludes with a discussion on the relationship between sequence, structure, and the number of protein folds over time.

Official source

Ontological neighbourhood

Biology

Cell biology: Protein biosynthesis

Related concepts (32)

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.

Protein biosynthesis

Protein biosynthesis (or protein synthesis) is a core biological process, occurring inside cells, balancing the loss of cellular proteins (via degradation or export) through the production of new proteins. Proteins perform a number of critical functions as enzymes, structural proteins or hormones. Protein synthesis is a very similar process for both prokaryotes and eukaryotes but there are some distinct differences. Protein synthesis can be divided broadly into two phases—transcription and translation.

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 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.

Related lectures (34)

Proteins: Central Dogma and Translation

Explains protein synthesis, translation, and the central dogma of molecular biology.

Protein Composition and Structure

Explores protein composition, peptide bonds, secondary structures, and protein folding prediction.

Proteins: Structure and Function

Explores the structure and function of proteins, emphasizing their diverse roles in living organisms.