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.
引用
收藏
页数:8
相关论文
共 50 条
  • [41] Interaction Dynamics of Intrinsically Disordered Proteins from Single-Molecule Spectroscopy
    Chowdhury, Aritra
    Nettels, Daniel
    Schuler, Benjamin
    ANNUAL REVIEW OF BIOPHYSICS, 2023, 52 : 433 - 462
  • [42] Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins
    Alston, Jhullian J.
    Soranno, Andrea
    Holehouse, Alex S.
    METHODS, 2021, 193 : 116 - 135
  • [43] Link node: A method to characterize the chain topology of intrinsically disordered proteins
    Lang, Danqi
    Chen, Le
    Zhang, Moxin
    Song, Haoyu
    Li, Jingyuan
    QUANTITATIVE BIOLOGY, 2025, 13 (03)
  • [44] Protein local conformations analyses in ordered and intrinsically disordered proteins in the light of a structural alphabet
    de Brevern, Alexandre G.
    PROTEIN SCIENCE, 2021, 30 : 50 - 51
  • [45] STRUCTURAL INFLUENCE OF TYROSYL IODINATION IN PROTEINS BY CIRCULAR-DICHROISM SPECTROSCOPY
    WALTON, AG
    HURWITZ, FI
    BIOPHYSICAL JOURNAL, 1979, 25 (02) : A57 - A57
  • [46] A reference dataset for circular dichroism spectroscopy tailored for the βγ-crystallin lens proteins
    Evans, P.
    Bateman, O. A.
    Slingsby, C.
    Wallace, B. A.
    EXPERIMENTAL EYE RESEARCH, 2007, 84 (05) : 1001 - 1008
  • [47] A reference dataset for the analyses of membrane protein secondary structures and transmembrane residues using circular dichroism spectroscopy
    Abdul-Gader, Ali
    Miles, Andrew John
    Wallace, B. A.
    BIOINFORMATICS, 2011, 27 (12) : 1630 - 1636
  • [48] Exploring intrinsically disordered proteins using site-directed spin labeling electron paramagnetic resonance spectroscopy
    Le Breton, Nolwenn
    Martinho, Marlene
    Mileo, Elisabetta
    Etienne, Emilien
    Gerbaud, Guillaume
    Guigliarelli, Bruno
    Belle, Valerie
    FRONTIERS IN MOLECULAR BIOSCIENCES, 2015, 2
  • [49] A New Method to Predict the Electronic Circular Dichroism Spectra of Proteins
    Nagy, Gabor
    Grubmueller, Helmut
    BIOPHYSICAL JOURNAL, 2017, 112 (03) : 290A - 290A
  • [50] Structure and Transition Dynamics of Intrinsically Disordered Proteins Probed by Single-Molecule Spectroscopy
    Pramanik, Ushasi
    Nandy, Atanu
    Khamari, Laxmikanta
    Mukherjee, Saptarshi
    LANGMUIR, 2022, 38 (42) : 12764 - 12772