# 1H, 15N, and 13C Resonance Assignment of Human Heat Shock Protein 10

## TL;DR

This paper provides the NMR resonance assignments for human Hsp10, a co-chaperone involved in protein folding, to better understand its structure and function.

## Contribution

The study presents the near-complete NMR backbone assignment of human Hsp10, enabling future structural and functional investigations.

## Key findings

- The 1H, 15N, and 13C resonance assignments for human Hsp10 were nearly complete.
- The results provide a foundation for studying Hsp10's role in protein folding and disease.
- Hsp10 may have regulatory functions beyond its traditional passive role in the chaperonin system.

## Abstract

The human chaperonin system, Hsp60/Hsp10, is essential for maintaining protein homeostasis and is found mainly in mitochondria. Hsp60 forms a bowl-shaped structure that provides an enclosed environment for protein folding, while its co-chaperone, Hsp10, acts as a cap to seal the barrel. This coordinated process is crucial for the proper folding of many unfolded or misfolded proteins, making the Hsp60/Hsp10 complex an indispensable chaperone system. Changes in their expression levels have been linked to diseases such as neurodegenerative disorders and cancer. Although Hsp60 has gained increasing attention, its co-chaperone Hsp10 remains relatively underexplored and has often been assumed to play a passive role. However, emerging studies challenge this view, suggesting that Hsp10 alone may exert regulatory functions within the chaperonin cycle. Here, we present the near-complete NMR backbone assignment of the 102-residue human Hsp10, laying the groundwork for future investigations into its structure, interactions, and roles in facilitating protein folding and preventing aggregation.