The insertion sequence of the N2A region of titin exists in an extended structure with helical characteristics

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• 作者：Holly Tiffany^b ; Kanchan Sonkar^a ; ¹ ; Matthew J. Gage^a ; ^c ; ^d ; ^{Matthew_Gage@UML.edu}
• 关键词：AMP ; ampicillin ; CD ; circular dichroism ; CFP ; cyan fluorescent protein ; Chlor ; chloramphenicol ; FRET ; fluorescence resonance energy transfer ; Ig ; immunoglobulin ; IPTG ; isopropyl β-D-1-thiogalactopyranoside ; LB ; Luria broth ; MARP2 ; muscle ankyrin repeat protein 2 ; N2A-IS ; 117 amino acid insertion sequence in N2A region of titin ; SEC ; size exclusion chromatography ; TFE ; 2 ; 2 ; 2-trifluoroethanol ; YFP ; yellow fluorescent protein
• 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1865
• 期：1
• 页码：1-10
• 全文大小：921 K
• 卷排序：1865

文摘

The N2A-IS region contains 15% α-helix. 2,2,2-Trifluoroethanol induces additional helical character in N2A-IS. The 13.9 kDa N2A-IS migrates as a 45 kDa protein on size exclusion chromatography. N2A-IS does not exhibit cooperative unfolding or folding. N2A-IS has a mean end-to-end distance of 5.2 nm as measured by FRET.