Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions
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- 作者：Karen Glover ; Yang Mei ; Sangita C. Sinha ; Sangita.Sinha@ndsu.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：IDR ; intrinsically disordered region ; TFE ; 2 ; 2 ; 2-trifluoroethanol ; MoRF ; molecular recognition feature ; CD ; circular dichroism ; FHD ; Flexible Helical Domain
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：October 2016
- 年：2016
- 卷：1864
- 期：10
- 页码：1455-1463
- 全文大小：847 K
文摘
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Many proteins contain intrinsically disordered regions (IDRs) that lack stable secondary or ordered tertiary structure.
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IDRs are often implicated in macromolecular interactions, and may undergo structural transitions upon binding.
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IDRs that undergo disorder-to-helix transitions can be identified by combined bioinformatics and experimental methods.
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The experimental methods use CD to assess stabilization of helical structure using 2,2,2-trifluoroethanol.