defining-hsp33-s-redox-regulated-chaperone-activity-mapping

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Living organisms regularly need to cope with fluctuating environments during their life cycle, including changes in temperature, pH, the accumulation of ...

The Hebrew University of Jerusalem

A recently discovered group of conditionally disordered chaperones share a very unique feature; they need to lose structure to become active as chaperones. This activation mechanism makes these chaperones particularly suited to respond to protein-unfolding stress conditions, such as oxidative unfolding. However, the role of this disorder in stress-related activation, chaperone function, and the crosstalk with other chaperone systems is not yet clear. Here, we focus on one of the members of the conditionally disordered chaperones, a thiol-redox switch of the bacterial proteostasis system, Hsp33.

A Role of Metastable Regions and Their Connectivity in the Inactivation of a Redox-Regulated Chaperone and Its Inter-Chaperone Crosstalk.

Kinetic measurements have played an important role in elucidating biochemical and biophysical phenomena for over a century. While many tools for analysing kinetic measurements exist, most require low noise levels in the data, leaving outlier measurements to be cleaned manually. This is particularly true for protein misfolding and aggregation processes, which are extremely noisy and hence difficult to model. Understanding these processes is paramount, as they are associated with diverse physiological processes and disorders, most notably neurodegenerative diseases. Therefore, a better tool for analysing and cleaning protein aggregation traces is required.

Oded Rimon

Department of Biological Chemistry,
The Alexander Silberman Institute of Life Sciences,
Safra Campus Givat Ram,
Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Safra Campus Givat Ram

The Hebrew University of Jerusalem

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Oded Rimon

.css-o250i3{font-size:18px;font-family:Open Sans,sans-serif;line-height:21.6px;}Department of Biological Chemistry,The Alexander Silberman Institute of Life Sciences,Safra Campus Givat Ram,Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Safra Campus Givat Ram

The Hebrew University of Jerusalem

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Department of Biological Chemistry,
The Alexander Silberman Institute of Life Sciences,
Safra Campus Givat Ram,
Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Safra Campus Givat Ram