Lecture

Protein Structure and Function: Folding and Degradation

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Description

This lecture focuses on the life cycle of proteins, emphasizing their folding, maturation, and degradation processes. It begins with a review of protein translation and the emergence of their three-dimensional structures. The instructor explains the different levels of protein structure, including primary, secondary, tertiary, and quaternary structures, and discusses the interactions that stabilize these formations, such as covalent bonds, ionic bonds, and hydrophobic interactions. The role of chaperones in assisting proper protein folding is highlighted, detailing how they prevent misfolding and aggregation. The lecture also addresses the consequences of incorrect folding, including the formation of toxic aggregates and their association with various neurodegenerative diseases, such as Alzheimer's, Parkinson's, and prion diseases. The importance of maintaining protein integrity within the cell is underscored, as misfolded proteins can lead to severe cellular dysfunction. Overall, the lecture provides a comprehensive overview of protein dynamics and their critical roles in cellular health.

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Official source

Ontological neighbourhood

Chemistry

Biochemistry: Proteins

Health sciences

Neurology: Neurodegenerative disease

Related concepts (32)

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 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 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.

Biomolecular structure

Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function. The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits. This useful distinction among scales is often expressed as a decomposition of molecular structure into four levels: primary, secondary, tertiary, and quaternary.

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.

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