NIH VideoCast - Quality Control of Transmembrane Proteins

Skip Navigation

Quality Control of Transmembrane Proteins

0 seconds of 53 minutes, 44 secondsVolume 90%

00:25

00:00

53:44

Air date:	Wednesday, March 23, 2005, 3:00:00 PM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 142 * This only includes stats from October 2011 and forward.
Category:	WALS - Wednesday Afternoon Lectures
Runtime:	00:53:45
Closed captioning:	Check box to display CC outside of the video Note: You can drag the captioning window around and resize it
Description:	Cells maintain their integrity by constantly seeking out and degrading damaged or misfolded proteins. For proteins in solution, it is the exposure of hydrophobic amino acids that normally are buried in the interior that signifies misfolding, and it is these that are recognised by molecular chaperones. For the lipid-embedded portions of transmembrane proteins, the converse holds – exposure of hydrophilic residues to the lipid bilayer can cause aggregation and is often sufficient to promote rapid degradation. Thus, for example, incompletely assembled forms of the T cell receptor (which is held together by polar interactions within the bilayer) are either held in the Endoplasmic Reticulum and degraded there, or transported to lysosomes for disposal. For more information, visit http://www2.mrc-lmb.cam.ac.uk/CB/Pelham_H/group/ WALS

Author:	Hugh Pelham, Ph.D., MRC Laboratory of Molecular Biology
CIT Live ID:	3447
Permanent link:	https://videocast.nih.gov/watch=3447

Related Videos...