Selected article for: "absolutely hydrophilic strongly polar and lys glu residue substitution"
Author: Hu, Yongwu; Wen, Jie; Tang, Lin; Zhang, Haijun; Zhang, Xiaowei; Li, Yan; Wang, Jing; Han, Yujun; Li, Guoqing; Shi, Jianping; Tian, Xiangjun; Jiang, Feng; Zhao, Xiaoqian; Wang, Jun; Liu, Siqi; Zeng, Changqing; Wang, Jian; Yang, Huanming
Title: The M Protein of SARS-CoV: Basic Structural and Immunological Properties
  • Document date: 2016_11_28
    • ID: xzlcyn3l_33
    Snippet: The first substitution is identified in the amino-terminal exterior region, at nucleotide position 26,409 of the entire genome and Codon 11 of the ORF for the M protein. It is a transition (G/A), leading to a residue substitution from Glu to Lys. Both are strongly polar and absolutely hydrophilic (100%) amino acids. However, the former is well known to be highly acidic (pI 4.50) and negatively charged, while the latter highly basic (pI 8.50) and .....
    Document: The first substitution is identified in the amino-terminal exterior region, at nucleotide position 26,409 of the entire genome and Codon 11 of the ORF for the M protein. It is a transition (G/A), leading to a residue substitution from Glu to Lys. Both are strongly polar and absolutely hydrophilic (100%) amino acids. However, the former is well known to be highly acidic (pI 4.50) and negatively charged, while the latter highly basic (pI 8.50) and positively charged. Therefore, the positional residue remains absolutely hydrophilic (100%), but alters the pI and charge of the protein. Consequently, a significant subregional alteration of pI (pI 4.20- 4.80) and charge (+/- from 5.6/22.2 to 11.1/16.7) caused by the substitution could be predicted for the exterior region (Codons 1-18) of the virion. It is known that high pI value generates a stronger antigenicity, and thus enhanced antigenicity should be postulated for this substitution in the M protein.

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