Protein folding Inside the cell : Macromolecular crowding and protein aggregation / R. J. Ellis.

Format:

Video

Author/Creator:

Ellis, R. J., author.

Language:

English

Subjects (All):

Biomolecules--Analysis.

Biomolecules.

Protein folding.

Physical Description:

1 videorecording (42 min., 16 sec.) : sound, color

Other Title:

Protein folding Inside the cell

Place of Publication:

London : Henry Stewart Talks, 2007.

System Details:

video file

Contents:

Introduction

Macromolecular crowding and protein aggregation

Topics to be discussed

The principle of protein self-assembly

Protein binding of a newly synthesized polypeptide

Rubisco chloroplast protein

Rubisco large subunit binding protein

Discovery of the chaperonins

BiP binding of the heavy chain of immunoglobulin

Origins of the molecular chaperone concept (1)

Origins of the molecular chaperone concept (2)

The march of molecular chaperones

In vivo protein folding comparing to in vitro folding

Protein aggregation

A possible fate for all polypeptide

Two key properties

Macromolecular crowding

Major consequences of macromolecular crowding

The excluded volume effect

The effect of macromolecular crowding

Effects of crowding on reaction rate

Predicted effects of macromolecular crowding

Effect of crowding agents on refolding of lysozyme

Crowding promotes the formation of amyloid fibrils

Lysozyme avoid aggregation when folding in ER

The solution to aggregation- in small chaperons

The solution to aggregation- in large chaperons

Molecular chaperones

The molecular chaperone function.

Notes:

Description based on publisher supplied metadata and other sources.

Retrieved April 8, 2024, from https://hstalks.com/bs/438/.