DisPredict3.0: Prediction of intrinsically disordered regions/ proteins using protein language model

被引:1
|
作者
UI Kabir, Md Wasi [1 ]
Hoque, Md Tamjidul [1 ]
机构
[1] Univ New Orleans, Dept Comp Sci, New Orleans, LA 70148 USA
基金
美国国家卫生研究院;
关键词
Protein language models; Intrinsically disordered proteins; Predict disordered protein; Machine learning; ACCURATE; DATABASE; DISPROT;
D O I
10.1016/j.amc.2024.128630
中图分类号
O29 [应用数学];
学科分类号
070104 ;
摘要
Intrinsically disordered proteins (IDPs) or protein regions (IDRs) do not have a stable threedimensional structure, even though they exhibit important biological functions. They are structurally and functionally very different from ordered proteins and can cause many critical diseases. Accurate identification of disordered proteins/regions significantly impacts fields such as drug design, protein engineering, protein design, and related research. However, experimental identification of IDRs is complex and time-consuming, necessitating the development of an accurate and efficient computational method. The recent development of deep learning methods for protein language models shows the ability to learn evolutionary information from billions of protein sequences. This motivates us to develop a computational method, named DisPredict3.0, to predict proteins' disordered regions (IDRs) using evolutionary information from a protein language model. Compared to the state-of-the-art method in the CAID (2018) assessment, DisPredict3.0 has an improvement of 2.51 %, 16.13 %, 17.98 %, and 11.94 % in terms of AUC, F1score, MCC, and kappa, respectively. In addition, in the CAID-2 assessment (2022), DisPredict3.0 shows promising results and is ranked first for disorder residue prediction on the Disorder-NOX dataset. The DisPredict3.0 webserver is available at https://bmll.cs.uno.edu.
引用
收藏
页数:14
相关论文
共 50 条
  • [21] Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell
    Deiana, Antonio
    Forcelloni, Sergio
    Porrello, Alessandro
    Giansanti, Andrea
    PLOS ONE, 2019, 14 (08):
  • [22] Computational prediction of functions of intrinsically disordered regions
    Katuwawala, Akila
    Ghadermarzi, Sina
    Kurgan, Lukasz
    DANCING PROTEIN CLOUDS: INTRINSICALLY DISORDERED PROTEINS IN HEALTH AND DISEASE, PT A, 2019, 166 : 341 - 369
  • [23] Verification of the Stabilized Protein Design Based on the Prediction of Intrinsically Disordered Regions: Ribosomal Proteins L1
    Nagibina, G. S.
    Marchenkov, V. V.
    Glukhova, K. A.
    Melnik, T. N.
    Melnik, B. S.
    BIOCHEMISTRY-MOSCOW, 2020, 85 (01) : 90 - 98
  • [24] ANALYSIS OF INTRINSICALLY DISORDERED REGIONS IN PROTEINS USING RECURRENCE QUANTIFICATION ANALYSIS
    Kulkarni, Abhijit
    Karnik, Shreyas
    Angadi, Savita
    INTERNATIONAL JOURNAL OF BIFURCATION AND CHAOS, 2011, 21 (04): : 1193 - 1202
  • [25] Predicting protein intrinsically disordered regions by applying natural language processing practices
    Chakraborty, Rajkumar
    Hasija, Yasha
    SOFT COMPUTING, 2022, 26 (22) : 12343 - 12353
  • [26] Predicting protein intrinsically disordered regions by applying natural language processing practices
    Rajkumar Chakraborty
    Yasha Hasija
    Soft Computing, 2022, 26 : 12343 - 12353
  • [27] Verification of the Stabilized Protein Design Based on the Prediction of Intrinsically Disordered Regions: Ribosomal Proteins L1
    G. S. Nagibina
    V. V. Marchenkov
    K. A. Glukhova
    T. N. Melnik
    B. S. Melnik
    Biochemistry (Moscow), 2020, 85 : 90 - 98
  • [28] DisPredict: A Predictor of Disordered Protein Using Optimized RBF Kernel
    Iqbal, Sumaiya
    Hoque, Md Tamjidul
    PLOS ONE, 2015, 10 (10):
  • [29] Do sequence neighbours of intrinsically disordered regions promote structural flexibility in intrinsically disordered proteins?
    Basu, Sushmita
    Bahadur, Ranjit Prasad
    JOURNAL OF STRUCTURAL BIOLOGY, 2020, 209 (02)
  • [30] Hydrodynamic Radius Prediction of Intrinsically Disordered Proteins
    Ricard, Benjamin
    Tomasso, Maria
    Whitten, Steven
    FASEB JOURNAL, 2016, 30