Author: Zhao, Huabin; Ru, Binghua; Teeling, Emma C.; Faulkes, Christopher G.; Zhang, Shuyi; Rossiter, Stephen J.
Title: Rhodopsin Molecular Evolution in Mammals Inhabiting Low Light Environments Document date: 2009_12_16
ID: 02uqygfs_12
Snippet: We examined the following 13 amino acid sites that have been linked to spectral tuning in rhodopsin: 83, 96, 102, 122, 183, 194, 195, 253, 261, 289, 292, 299 and 317 [17, [23] [24] (listed in Table S4 ). We inferred the wavelength of maximum absorption (l max ) conferred by particular combinations of critical amino acids following published studies [14, 17, [23] [24] (see Table S4 ). Specifically, we assumed that the single amino acid replacemen.....
Document: We examined the following 13 amino acid sites that have been linked to spectral tuning in rhodopsin: 83, 96, 102, 122, 183, 194, 195, 253, 261, 289, 292, 299 and 317 [17, [23] [24] (listed in Table S4 ). We inferred the wavelength of maximum absorption (l max ) conferred by particular combinations of critical amino acids following published studies [14, 17, [23] [24] (see Table S4 ). Specifically, we assumed that the single amino acid replacements D83N, M183L, S299A would lead to downward shift of l max by 2 nm based on data from pinnipeds [24] , and we assumed that the single mutation L194P and double mutations D83N/L194P would result in downward shift of 3 and 5 nm, respectively, based on cetaceans [14] .
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