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Lecture

Protein Folding Dynamics

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 covers the intricate process of protein folding, including the role of chaperones, ATP hydrolysis, and the conformational changes that occur. It also delves into DNA folding, the impact of nucleotides, and the structural organization within the nucleus.

Official source

Ontological neighbourhood

Chemistry

Biochemistry: Proteins

Related concepts (32)

Chaperone (protein)

In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA.

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.

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 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.

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.

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Protein Folding: Mechanisms and Consequences

Explores protein folding, misfolding consequences, chaperones' role, and ATP importance.

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

Hsp70 Molecular Chaperones: Conformational Flexibility and Function

Explores the conformational and functional flexibility of Hsp70 molecular chaperones, focusing on folding intermediates and the Hsp70 functional cycle.

Protein-Repair Machineries: Evolution and Function

Explores the evolution and function of protein-repair machineries, emphasizing the role of ATP-fueled unfolding machines in preventing protein aggregation and promoting proper folding.

Protein Structure: General Principles