Chaperonin-mediated protein folding. 2 / Arthur Horwich.

Format:

Video

Author/Creator:

Horwich, Arthur, author.

Language:

English

Subjects (All):

Molecular chaperones.

Physical Description:

1 streaming video file (45 min.) : color, sound

Place of Publication:

London : Henry Stewart Talks Ltd, 2012.

System Details:

video file

Contents:

Introduction

Talk outline

Folding reaction (1)

Folding reaction (2)

Polypeptide folding (1)

Polypeptide folding (2)

Productive release from GroEL

Single ring versions of GroEL (1)

Single ring versions of GroEL (2)

ATP binding triggers productive folding

The 1996 team

A model of GroEL-GroES (1)

A model of GroEL-GroES (2)

A model of GroEL-GroES (3)

A model of GroEL-GroES (4)

A model of GroEL-GroES (5)

Permissive and non-permissive conditions

Rubisco folding under permissive conditions

Non-native rubisco folding free in solution

Chaperonin-mediated refolding of DM-MBP

DM-MBP refolding is concentration-dependent

DM-MBP refolding produces light scattering

Absence of chloride (Cl) relieves light scattering

Absence of Cl relieves concentration dependence

Permissive conditions

Ben Schuler's group observations

AlFx addition triggers productive folding

ATP analogue bound in GroEL nucleotide pocket

Distance measurements

Substrate presents "load" on apical domain

Dome formation

The proceeding nucleotide cycle

Binding to trans ring requires hydrolysis in cis

Steps of formation of the domed chamber

Energy transfer experiments

Trans association experiments (1)

Trans association experiments (2)

Summary of the reaction cycle

GroEL animation (1)

GroEL animation (2)

Acknowledgements (1)

Acknowledgements (2).

Notes:

Description based on publisher supplied metadata and other sources.

Retrieved April 15, 2024, from https://hstalks.com/bs/2389/.