ArticleProceedings of the National Academy of Sciences of the United States of America2012
Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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59 citing papers in PubMed, 134 citations in OpenAlex.
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- AggNet: Advancing protein aggregation analysis through deep learning and protein language model.Protein science : a publication of the Protein Society · 2025Article
- Unravelling γD-crystallin aggregation pathway to understand cataract formation using fluorescence correlation spectroscopy.Molecular vision · 2025Article
- Unravelling γD-crystallin aggregation pathway to understand cataract formation using fluorescence correlation spectroscopy.Molecular vision · 2025Article
- Probing local changes to α-helical structures with 2D IR spectroscopy and isotope labeling.Biophysical journal · 2023Article
- Frequency Changes in Terminal Alkynes Provide Strong, Sensitive, and Solvatochromic Raman Probes of Biochemical Environments.The journal of physical chemistry. B · 2023Article
- Investigating the effects of N-terminal acetylation on KFE8 self-assembly with 2D IR spectroscopy.Biophysical journal · 2022Article
- Segmental and site-specific isotope labelling strategies for structural analysis of posttranslationally modified proteins.RSC chemical biology · 2021Review
- Coupling chemical biology and vibrational spectroscopy for studies of amyloids in vitro and in cells.Current opinion in chemical biology · 2021Review
- Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- Membrane-dependent amyloid aggregation of human BAX α9 (173-192).Protein science : a publication of the Protein Society · 2021Article
- Mechanism of human γD-crystallin protein aggregation in UV-C light.Molecular vision · 2021Article
- Vibrational Spectroscopic Map, Vibrational Spectroscopy, and Intermolecular Interaction.Chemical reviews · 2020Review
- Unraveling VEALYL Amyloid Formation Using Advanced Vibrational Spectroscopy and Microscopy.Biophysical journal · 2020Article
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- Application of Circular Dichroism and Fluorescence Spectroscopies To Assess Photostability of Water-Soluble Porcine Lens Proteins.ACS omega · 2020Article
- Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents.PLoS pathogens · 2019Article
- Site-Specific 1D and 2D IR Spectroscopy to Characterize the Conformations and Dynamics of Protein Molecular Recognition.The journal of physical chemistry. B · 2019Article
- Amyloid found in human cataracts with two-dimensional infrared spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Vibrational Approach to the Dynamics and Structure of Protein Amyloids.Molecules (Basel, Switzerland) · 2019Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structural eye lens protein γD-crystallin is a major component of cataracts, but its conformation when aggregated is unknown. Using expressed protein ligation, we uniformly (13)C labeled one of the two Greek key domains so that they are individually resolved in two-dimensional (2D) IR spectra for structural and kinetic analysis. Upon acid-induced amyloid fibril formation, the 2D IR spectra reveal that the C-terminal domain forms amyloid β-sheets, whereas the N-terminal domain becomes extremely disordered but lies in close proximity to the β-sheets. Two-dimensional IR kinetics experiments show that fibril nucleation and extension occur exclusively in the C-terminal domain. These results are unexpected because the N-terminal domain is less stable in the monomer form. Isotope dilution experiments reveal that each C-terminal domain contributes two or fewer adjacent β-strands to each β-sheet. From these observations, we propose an initial structural model for γD-crystallin amyloid fibrils. Because only 1 μg of protein is required for a 2D IR spectrum, even poorly expressing proteins can be studied under many conditions using this approach. Thus, we believe that 2D IR and protein ligation will be useful for structural and kinetic studies of many protein systems for which IR spectroscopy can be straightforwardly applied, such as membrane and amyloidogenic proteins.
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