scholarly journals Statistical-thermodynamic model for light scattering from eye lens protein mixtures

2017 ◽  
Vol 146 (5) ◽  
pp. 055101 ◽  
Author(s):  
Michael M. Bell ◽  
David S. Ross ◽  
Maurino P. Bautista ◽  
Hossein Shahmohamad ◽  
Andreas Langner ◽  
...  
Keyword(s):  
Light Scattering ◽  
Thermodynamic Model ◽  
Statistical Thermodynamic ◽  
Eye Lens ◽  
Lens Protein ◽  
Eye Lens Protein

scholarly journals Catalysis of cataract-associated human γD crystallin aggregation via dynamic disulfide exchange

2018 ◽  
Author(s):  
Eugene Serebryany ◽  
Shuhuai Yu ◽  
Sunia A. Trauger ◽  
Bogdan Budnik ◽  
Eugene I. Shakhnovich
Keyword(s):  
Light Scattering ◽  
Disulfide Bond ◽  
Eye Lens ◽  
Lens Protein ◽  
Biochemical Mechanism ◽  
Wild Type ◽  
Disulfide Exchange ◽  
Mechanism Of Catalysis ◽  
Eye Lens Protein

AbstractSeveral mutations in human γD-crystallin (HγD), a long-lived eye lens protein, cause misfolding and aggregation, leading to cataract. Surprisingly, wild-type HγD catalyzes aggregation of its cataract related W42Q variant while itself remaining soluble – the inverse of the classical prion-like scenario whereby misfolded polypeptides catalyze aggregation of natively folded ones. The search for a biochemical mechanism of catalysis of W42Q aggregation by WT has revealed that WT HγD can transfer a disulfide bond to the W42Q variant. The transferred disulfide kinetically traps an aggregation-prone intermediate made accessible by the W42Q mutation, facilitating light-scattering aggregation of the W42Q variant. The aggregating variant thus becomes a disulfide sink, removing the disulfides from solution. Such redox “hot potato” competitions among wild-type and mutant or modified polypeptides may be relevant for many long-lived proteins that function in oxidizing environments. In these cases aggregation may be forestalled by inhibiting disulfide flow toward damaged polypeptides.

scholarly journals Sticky-Sphere Mixture Model for Light Scattering from Concentrated Eye Lens Protein Mixtures

2013 ◽  
Vol 104 (2) ◽  
pp. 392a
Author(s):  
George M. Thurston ◽  
Michael M. Bell ◽  
David S. Ross ◽  
Maurino P. Bautista ◽  
Carrie N. Lahnovych
Keyword(s):  
Light Scattering ◽  
Mixture Model ◽  
Eye Lens ◽  
Lens Protein ◽  
Eye Lens Protein

Letter to the Editor: 1H, 15N and 13C resonance assignment of human ?S-crystallin, a 21�kDa eye-lens protein

2004 ◽  
Vol 30 (3) ◽  
pp. 385-386 ◽  
Author(s):  
Carine Baraguey ◽  
F�riel Skouri-Panet ◽  
Fran�ois Bontems ◽  
Annette Tardieu ◽  
G�rard Chassaing ◽  
...  
Keyword(s):  
Resonance Assignment ◽  
Eye Lens ◽  
Lens Protein ◽  
Letter To The Editor ◽  
Eye Lens Protein

scholarly journals e-Crystallin, a novel avian and reptilian eye lens protein

1985 ◽  
Vol 147 (1) ◽  
pp. 129-136 ◽  
Author(s):  
Steven O. STAPEL ◽  
Anneke ZWEERS ◽  
Huub J. DODEMONT ◽  
Jaap H. KAN ◽  
Wilfried W. JONG
Keyword(s):  
Eye Lens ◽  
Lens Protein ◽  
Eye Lens Protein

A new model linking elastic properties and ionic conductivity of mixed network former glasses

2018 ◽  
Vol 20 (3) ◽  
pp. 1629-1641 ◽  
Author(s):  
Weimin Wang ◽  
Randilynn Christensen ◽  
Brittany Curtis ◽  
Steve W. Martin ◽  
John Kieffer
Keyword(s):  
Light Scattering ◽  
Ionic Conductivity ◽  
Impedance Spectroscopy ◽  
Elastic Properties ◽  
Thermodynamic Model ◽  
Elastic Moduli ◽  
Statistical Thermodynamic ◽  
Systematic Comparison ◽  
New Model ◽  
Mixed Network

A new statistical thermodynamic model has been developed to describe the activated process of cation hopping in mixed network former glasses based on the systematic comparison between the adiabatic elastic moduli measured using Brillouin light scattering and the ionic conductivity measured using dielectric impedance spectroscopy.

Dietary Vitamin C Delays UV-induced Eye Lens Protein Damage

1987 ◽  
Vol 498 (1 Third Confere) ◽  
pp. 460-463 ◽  
Author(s):  
J. BLONDIN ◽  
V. BARAGI ◽  
E. R. SCHWARTZ ◽  
J. A. SADOWSKI ◽  
A. TAYLOR
Keyword(s):  
Vitamin C ◽  
Protein Damage ◽  
Dietary Vitamin ◽  
Eye Lens ◽  
Lens Protein ◽  
Eye Lens Protein
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