Alanine scanning effects on the biochemical and viophysical properties of intrinsically disordered proteins: a case study of the histidine to alanine mutations in amyloid-beta(42)
Yükleniyor...
Dosyalar
Tarih
2019
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Amer Chemical Soc
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
Alanine scanning is a tool in molecular biology that is commonly used to evaluate the contribution of a specific amino acid residue to the stability and function of a protein. Additionally, this tool is also used to understand whether the side chain of a specific amino acid residue plays a role in the protein's bioactivity. Furthermore, computational alanine scanning methods are utilized to predict the thermodynamic properties of proteins. These studies are utilized with the assumption that the biochemical and biophysical properties of a protein do not change with alanine scanning. Our study was dedicated to analyze the effect of alanine scanning on the biochemical and biophysical properties of intrinsically disordered proteins. To this end, we studied the impact of widely used histidine to alanine mutations in amyloid-beta (A beta). We found that the secondary and tertiary contacts, salt bridge formations, and thermodynamic properties, as well as disorder propensities and aggregation predisposition of A beta, are impacted by the single and triple point histidine to alanine mutations. Experimental and computational studies employing the alanine scanning technique for mutating histidine to alanine in the analysis of intrinsically disordered proteins have to consider these effects.
Açıklama
Uversky, Vladimir N./0000-0002-4037-5857; Coskuner, Orkid/0000-0002-0772-9350
WOS:000459948700023
PubMed: 30694660
WOS:000459948700023
PubMed: 30694660
Anahtar Kelimeler
Kaynak
Journal Of Chemical Information And Modeling
WoS Q Değeri
Q1
Scopus Q Değeri
Q1
Cilt
59
Sayı
2
