pone.0257098.s005.tif (1.84 MB)
A 2DIR and TEM comparison of αB-crystallin and αB-R120G-crystallin with acid treatment.
figure
posted on 2021-09-14, 17:23 authored by Ariel M. Alperstein, Kathleen S. Molnar, Sidney S. Dicke, Kieran M. Farrell, Leah N. Makley, Martin T. Zanni, Usha P. Andley(A) Overlay of diagonal slices for room temperature αB-crystallin (solid light blue, data in Fig 2A), heated sample (dashed light blue, data in Fig 2A), and acid treated sample (dotted light blue). Data has been normalized to 1639 cm−1 to match the room temperature sample. (B) Overlay of diagonal slices for room temperature αB-R120G-crystallin (solid maroon, data in Fig 2B), heated sample (dashed maroon, data in Fig 2B), and acid treated sample (dotted maroon). Data has been normalized to 1632 cm−1 to match the room temperature sample. (C) TEM image of acid treated αB-crystallin. Dark blue scale bar is 100 nm.
(TIF)
History
Usage metrics
Categories
Keywords
measure uv radiationdiv >< pdeveloping pharmacological treatmentscross peak frequencyalso widely distributedordered secondary structurelike secondary structurecross peak changesmutant mouse lensesrelated cataract diseaseprotein structural relevancediagonal peak frequenciesform amorphous aggregates>- r120g knockwt mouse lensesmouse lens modelhuman hereditary cataractsdimensional infrared spectroscopyhuman lensesdimensional infraredmouse modelporcine lensesocular lenslike fibrilsinduced changeshighly orderedhereditary cataracts>- r120gcrystallin aggregatesvitro tissues throughoutstudy ageneurodegenerative diseasesheterooligomeric complexgeneral agecryab chaperone activityarginine 120alzheimer ’aggregated proteins
Licence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC