Protein refractive index increment is determined by conformation as well as composition.

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ID: 59568
2018
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Ranked #10 of 53 articles by views in journal of physics condensed matter : an institute of physics journal

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Abstract
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.
Reference Key
khago2018proteinjournal Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Khago, Domarin;Bierma, Jan C;Roskamp, Kyle W;Kozlyuk, Natalia;Martin, Rachel W;
Journal journal of physics condensed matter : an institute of physics journal
Year 2018
DOI
10.1088/1361-648X/aae000
URL
Keywords
DFT molecular descriptors computational study nitrogen compounds

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