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DichroIDP: a method for analyses of intrinsically disordered proteins using circular dichroism spectroscopy
被引:15
|作者:
Miles, Andrew J. J.
[1
]
Drew, Elliot D. D.
[2
,3
]
Wallace, B. A.
[1
]
机构:
[1] Birkbeck Univ London, Inst Struct & Mol Biol, London WC1E 7HX, England
[2] Queen Mary Univ London, Sch Biol & Chem Sci, Mile End Rd, London E1 4NS, England
[3] Zappi, London NW1 7JN, England
基金:
英国生物技术与生命科学研究理事会;
关键词:
SECONDARY STRUCTURE;
SYNCHROTRON-RADIATION;
STRUCTURE PREDICTION;
STANDARDIZATION;
RECOGNITION;
CALIBRATION;
SPECTRA;
FOLD;
D O I:
10.1038/s42003-023-05178-2
中图分类号:
Q [生物科学];
学科分类号:
07 ;
0710 ;
09 ;
摘要:
Intrinsically disordered proteins (IDPs) are comprised of significant numbers of residues that form neither helix, sheet, nor any other canonical type of secondary structure. They play important roles in a broad range of biological processes, such as molecular recognition and signalling, largely due to their chameleon-like ability to change structure from unordered when free in solution to ordered when bound to partner molecules. Circular dichroism (CD) spectroscopy is a widely-used method for characterising protein secondary structures, but analyses of IDPs using CD spectroscopy have suffered because the methods and reference datasets used for the empirical determination of secondary structures do not contain adequate representations of unordered structures. This work describes the creation, validation and testing of a standalone Windows-based application, DichroIDP, and a new reference dataset, IDP175, which is suitable for analyses of proteins containing significant amounts of disordered structure. DichroIDP enables secondary structure determinations of IDPs and proteins containing intrinsically disordered regions. DichroIDP is a method with a bespoke reference dataset for analyzing and determining secondary structures in proteins containing intrinsically disordered regions using circular dichroism spectroscopy.
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页数:8
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