Macromolecular crowding effects on the intrinsically disordered proteins: A simple model reveals complex behavior

被引：0
|
作者：
Kim, Youngchan [2 ]
Miller, Cayla [3 ]
Mittal, Jeetain [1 ]
机构：
[1] Lehigh Univ, Bethlehem, PA 18015 USA
[2] NRL, Code 6390, Washington, DC USA
[3] Stanford Univ, Stanford, CA 94305 USA
来源：
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY | 2016年 / 252卷
关键词：
D O I：
暂无
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
210
引用
收藏
页数：1
相关论文
共 50 条
  • [1] Crowding effects on intrinsically disordered proteins
    Thirumalai, Dave
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2016, 252
  • [2] Influence of macromolecular crowding on the charge regulation of intrinsically disordered proteins
    Blanco, Pablo M.
    Madurga, Sergio
    Garces, Josep L.
    Mas, Francesc
    Dias, Rita S.
    SOFT MATTER, 2021, 17 (03) : 655 - 669
  • [3] Macromolecular Crowding and Intrinsically Disordered Proteins: A Polymer Physics Perspective
    Cubuk, Jasmine
    Soranno, Andrea
    CHEMSYSTEMSCHEM, 2022, 4 (05)
  • [4] Effects of Molecular Crowding on the Dynamics of Intrinsically Disordered Proteins
    Cino, Elio A.
    Karttunen, Mikko
    Choy, Wing-Yiu
    PLOS ONE, 2012, 7 (11):
  • [5] Effects of Macromolecular Crowding on the Conformational Ensembles of Disordered Proteins
    Qin, Sanbo
    Zhou, Huan-Xiang
    JOURNAL OF PHYSICAL CHEMISTRY LETTERS, 2013, 4 (20): : 3429 - 3434
  • [6] Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27Kip1
    Flaugh, SL
    Lumb, KJ
    BIOMACROMOLECULES, 2001, 2 (02) : 538 - 540
  • [7] Concentrated Solutions of Single-Chain Nanoparticles: A Simple Model for Intrinsically Disordered Proteins under Crowding Conditions
    Moreno, Angel J.
    Lo Verso, Federica
    Arbe, Arantxa
    Pomposo, Jose A.
    Colmenero, Juan
    JOURNAL OF PHYSICAL CHEMISTRY LETTERS, 2016, 7 (05): : 838 - 844
  • [8] Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding
    Vladimir N. Uversky
    The Protein Journal, 2009, 28 : 305 - 325
  • [9] Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding
    Uversky, Vladimir N.
    PROTEIN JOURNAL, 2009, 28 (7-8): : 305 - 325
  • [10] Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding
    Banks, Anthony
    Qin, Sanbo
    Weiss, Kevin L.
    Stanley, Christopher B.
    Zhou, Huan-Xiang
    BIOPHYSICAL JOURNAL, 2018, 114 (05) : 1067 - 1079
12345