O
Olutayo Ogun
Researcher at Massachusetts Institute of Technology
Publications - 24
Citations - 1932
Olutayo Ogun is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Lens protein & Crystallin. The author has an hindex of 21, co-authored 24 publications receiving 1828 citations.
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Journal ArticleDOI
Binary-liquid phase separation of lens protein solutions.
TL;DR: By comparing the published protein sequences for calf, rat, and human gamma-crystallins, it is postulate that a few key amino acid residues account for the division of gamma- Crystallins into low-Tc and high-TC groups.
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Crystal cataracts: Human genetic cataract caused by protein crystallization
Ajay Pande,Jayanti Pande,Neer Asherie,Aleksey Lomakin,Olutayo Ogun,Jonathan King,George B. Benedek +6 more
TL;DR: A molecular basis for lens opacity in two genetic cataracts is provided and it is suggested that the opacity occurs because of the spontaneous crystallization of the mutant proteins.
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High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract.
Ajit K. Basak,Orval A. Bateman,Christine Slingsby,Ajay Pande,Neer Asherie,Olutayo Ogun,George B. Benedek,Jayanti Pande +7 more
TL;DR: The results presented here are the first high-resolution X-ray structures of human gamma crystallins and conclude that the reduction in the solubility of the mutant is mainly due to the effect of the R58H mutation in the solution phase.
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Effect of polyethylene glycol on the liquid–liquid phase transition in aqueous protein solutions
Onofrio Annunziata,Neer Asherie,Aleksey Lomakin,Jayanti Pande,Olutayo Ogun,George B. Benedek +5 more
TL;DR: The measurements of both LLPS temperature and PEG partitioning in the ternary γD-PEG-water systems are used to successfully predict the location of the liquid–liquid phase boundary of the binary γ D-water system and can be also used to estimate the protein solubility as a function of the concentration of crystallizing agents.
Journal ArticleDOI
Solid-liquid phase boundaries of lens protein solutions.
Carolyn R. Berland,George M. Thurston,Mamoru Kondo,Michael L. Broide,Jayanti Pande,Olutayo Ogun,George B. Benedek +6 more
TL;DR: Over the range of concentration and temperature for which liquid-liquid phase separation occurs, the coexistence of a protein crystal phase with a protein liquid solution phase is thermodynamically stable relative to the metastable separated liquid phases.