Protein refractive index increment is determined by conformation as well as composition
Autor: | Rachel W. Martin, Jan C. Bierma, Kyle W. Roskamp, Natalia Kozlyuk, Domarin Khago |
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Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Abundance (chemistry) Protein Conformation Fluids & Plasmas Analytical chemistry Article 03 medical and health sciences Polarizability Crystallin medicine Animals Humans Nanotechnology General Materials Science Eye Disease and Disorders of Vision chemistry.chemical_classification refractive index increment refractive index 030102 biochemistry & molecular biology Component (thermodynamics) Materials Engineering Condensed Matter Physics Crystallins Amino acid Solvent Refractometry 030104 developmental biology medicine.anatomical_structure chemistry Lens (anatomy) eye lens proteins protein Refractive index |
Zdroj: | Journal of physics. Condensed matter : an Institute of Physics journal, vol 30, iss 43 |
Popis: | The refractive index gradient of the eye lens is controlled by the concentration and distribution of its component crystallin proteins, which are highly enriched in polarizable amino acids. The current understanding of the refractive index increment ([Formula: see text]) of proteins is described using an additive model wherein the refractivity and specific volume of each amino acid type contributes according to abundance in the primary sequence. Here we present experimental measurements of [Formula: see text] for crystallins from the human lens and those of aquatic animals under uniform solvent conditions. In all cases, the measured values are much higher than those predicted from primary sequence alone, suggesting that structural factors also contribute to protein refractive index. |
Databáze: | OpenAIRE |
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