ArticleProtein science : a publication of the Protein Society2011
Contributions of aromatic pairs to the folding and stability of long-lived human γD-crystallin.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 47 citations in OpenAlex.
- Review
- Human γS-Crystallin Mutation F10_Y11delinsLN in the First Greek Key Pair Destabilizes and Impairs Tight Packing Causing Cortical Lamellar Cataract.International journal of molecular sciences · 2023Article
- The Y46D Mutation Destabilizes Dense Packing of the Second Greek Key Pair of Human γC-Crystallin Causing Congenital Nuclear Cataracts.Biochemistry · 2023Article
- Insights to Human γD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations.International journal of molecular sciences · 2022Article
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- Evaluation of the roles of hydrophobic residues in the N-terminal region of archaeal trehalase in its folding.Applied microbiology and biotechnology · 2021Article
- Function and Aggregation in Structural Eye Lens Crystallins.Accounts of chemical research · 2020Review
- Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation.The Journal of biological chemistry · 2018Article
- Thermodynamic and fibril formation studies of full length immunoglobulin light chain AL-09 and its germline protein using scan rate dependent thermal unfolding.Biophysical chemistry · 2015Article
- Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy.The Journal of biological chemistry · 2014Article
- The βγ-crystallins: native state stability and pathways to aggregation.Progress in biophysics and molecular biology · 2014Review
- Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutants.Protein science : a publication of the Protein Society · 2014Article
- Tyrosine/cysteine cluster sensitizing human γD-crystallin to ultraviolet radiation-induced photoaggregation in vitro.Biochemistry · 2014Article
- Comparative analysis of human γD-crystallin aggregation under physiological and low pH conditions.PloS one · 2014Article
- Dissecting the contributions of β-hairpin tyrosine pairs to the folding and stability of long-lived human γD-crystallins.Nanoscale · 2014Article
- Study of the γD-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: experiment and simulation.The journal of physical chemistry. B · 2013Article
- The Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of β-Sheets.Journal of molecular biology · 2013Article
- Structural integrity of the Greek key motif in βγ-crystallins is vital for central eye lens transparency.PloS one · 2013Article
- Functionally important aromatic-aromatic and sulfur-π interactions in the D2 dopamine receptor.Journal of the American Chemical Society · 2012Article
- Protein misfolding and aggregation in cataract disease and prospects for prevention.Trends in molecular medicine · 2012Review
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2 authors at 1 institution in 1 country.
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Abstract
Human γD-crystallin (HγD-Crys) is a highly stable protein that remains folded in the eye lens for the majority of an individual's lifetime. HγD-Crys exhibits two homologous crystallin domains, each containing two Greek key motifs with eight β-strands. Six aromatic pairs (four Tyr/Tyr, one Tyr/Phe and one Phe/Phe) are present in the β-hairpin sequences of the Greek keys. Ultraviolet damage to the aromatic residues in lens crystallins may contribute to the genesis of cataract. Mutant proteins with these aromatic residues substituted with alanines were constructed and expressed in E. coli. All mutant proteins except F115A and F117A had lower thermal stability than the WT protein. In equilibrium experiments in guanidine hydrochloride (GuHCl), all mutant proteins had lower thermodynamic stability than the WT protein. N-terminal domain (N-td) substitutions shifted the N-td transition to lower GuHCl concentration, but the C-terminal domain (C-td) transition remained unaffected. C-td substitutions led to a more cooperative unfolding/refolding process, with both the N-td and C-td transitions shifted to lower GuHCl concentration. The aromatic pairs conserved for each Greek key motif (Greek key pairs) had larger contributions to both thermal stability and thermodynamic stability than the other pairs. Aromatic-aromatic interaction was estimated as 1.5-2.0 kcal/mol. In kinetic experiments, N-td substitutions accelerated the early phase of unfolding, while C-td substitutions accelerated the late phase, suggesting independent domain unfolding. Only substitutions of the second Greek key pair of each crystallin domain slowed refolding. The second Greek keys may provide nucleation sites during the folding of the double-Greek-key crystallin domains.
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