Scholarlink

Abstract <p>Disordered proteins are of great interest due to their structural features, as they do not have well-defined three-dimensional structures. These proteins, often called intrinsically disordered proteins or regions, play critical roles in various cellular processes and are associated with the development of a number of diseases. Our in silico research focused on the investigation of protein complexes that include both ordered proteins, such as 14-3-3γ, and proteins containing intrinsically disordered regions, such as nucleocapsid (N) of SARS-CoV-2 and p53. Our findings demonstrate, that complexes modeled by AlphaFold2 and refined using discrete molecular dynamics simulations acquire assembled structures in disordered regions. After refinement, the modeled complexes exhibit a degree of structural assembly that addresses a key challenge in studying disordered proteins—their propensity to evade stable conformations.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

πDMD Simulation as a Strategy for Refinement of AlphaFold2 Modeled Fuzzy Protein Complexes Structures

  • 期刊论文

  • 发表日期：

    2025年2月20日

查看全文
  • N. G. Muradyan,
  • A. A. Sargsyan,
  • V. G. Arakelov,
  • A. K. Paronyan,
  • G. G. Arakelov,
  • K. B. Nazaryan

摘要

Abstract

Disordered proteins are of great interest due to their structural features, as they do not have well-defined three-dimensional structures. These proteins, often called intrinsically disordered proteins or regions, play critical roles in various cellular processes and are associated with the development of a number of diseases. Our in silico research focused on the investigation of protein complexes that include both ordered proteins, such as 14-3-3γ, and proteins containing intrinsically disordered regions, such as nucleocapsid (N) of SARS-CoV-2 and p53. Our findings demonstrate, that complexes modeled by AlphaFold2 and refined using discrete molecular dynamics simulations acquire assembled structures in disordered regions. After refinement, the modeled complexes exhibit a degree of structural assembly that addresses a key challenge in studying disordered proteins—their propensity to evade stable conformations.