Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2009 Jul 28;15:1429–1444.

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Comparison of chaperone activities of wild-type αB-crystallin and its mutants under thermal denaturation. A: Porcine α-crystallin was used as a substrate for chaperone-activity assays of wild-type αB-crystallin and mutants at 65 °C. Mutant proteins and wild-type αB-crystallin showed different chaperone activities at a molar ratio of 2:3 (chaperone/γ-crystallin). The scattering curves at 360 nm in the presence of chaperoning crystallins are shown as follows: control solution without chaperone (closed square), wild-type αB-crystallin (closed circle), Δ1 (closed triangle), Δ2 (closed asterisk), Δ1/K174A (open square), K174A (open circle), K175A (open triangle), and K174/175A (open asterisk). It is noted that K174/175A and Δ1/K174A show the highest activity among all mutants. B: Comparison of chaperone activities of wild-type αB-crystallin and mutants with different electrostatic amino acids under identical conditions as in A. The scattering curves at 360 nm in the presence of chaperoning crystallins are shown as follows: control solution without chaperone (closed square), wild-type αB-crystallin (closed circle), Δ1 (closed triangle), Δ2 (closed rhombus), Δ1/K174A (open square), Δ1/K174S (open circle), Δ1/K174E (open triangle), K174/175A (open rhombus), and K174/175E (open asterisk). C: Comparison of chaperone activity (percentage protection) of wild-type αB-crystallin and mutants. Wild-type αB-crystallin was shown to possess poor protective activity and K174/175E shown to possess the best protective activity among all proteins. The final concentration of porcine α-crystallin is 5.5 μM. D: Chaperone activities of wild-type αB-crystallin and its mutants under thermal denaturation at 70 °C. Porcine α-crystallin was used as a substrate for chaperone-activity assays of wild-type αB-crystallin and its mutants with different electrostatic amino acids at 70 °C in a molar ratio of 2:3 (chaperone/γ-crystallin). The scattering curves at 360 nm in the presence of chaperoning crystallins are shown as follows: control solution without chaperone (closed square), wild-type αB-crystallin (closed circle), Δ1 (closed triangle), Δ2 (closed rhombus), Δ1/K174A (open square), Δ1/K174S (open circle), Δ1/K174E (open triangle), K174/175A (open rhombus), and K174/175E (open asterisk). Both Δ1/K174E and K174/175E show the best protective activity among all mutants under these conditions. The final concentration of porcine α-crystallin is 5.5 μM.