Protein folding in vivo / Prof. James Bardwell.

Format:

Video

Author/Creator:

Bardwell, Prof. James, author.

Language:

English

Subjects (All):

Protein folding.

Physical Description:

1 videorecording (37 min., 54 sec.)

Place of Publication:

London : Henry Stewart Talks Ltd, 2012.

System Details:

video file

Contents:

Introduction

Protein folding in vitro

Protein folding in vivo

Interests

Chaperones

HdeA protects E. coli from stomach acid

E. coli under non-stress conditions

HdeA mechanism

FRET to monitor HdeA conformation

HdeA unfolding monitored by FRET

HdeA adaptively binds substrates

HdeA releases substrates very slowly

Monitoring structural changes in HdeA

Examine HdeA

Examine substrate

In vivo folding

Ways to measure folding and stability

To better understand in vivo folding

A tripartite fusion system

Quantitative in vivo stability readout

Proteins inserted into beta-lactamase

Selection for stabilized IM7 variants

PenV-resistant IM7 mutants are stabilized

Most proteins are only marginally stable

Why are proteins so unstable?

Stabilizing mutations map to binding interface

Optimizing folding in vivo

A dual selection system

Effect instability of the inserted protein

Fold or die!

IM7 and Spy in the periplasm of EMS strains

BaeS regulates Spy

Spy overproduction is sufficient to stabilize IM7

Spy inhibits MDH aggregation

Spy suppresses protein aggregation

Spy enhances protein refolding

Spy and tannins

Spy forms a thin cradle shaped dimer

Substrate binding and environment changes

Optimization of in vivo folding

Acknowledgments.

Notes:

Description based on publisher supplied metadata and other sources.

Retrieved April 13, 2024, from https://hstalks.com/bs/2235/.