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The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
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The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
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Characterizing Aciniform Silk Repetitive Domain Backbone Dynamics and Hydrodynamic Modularity.

Marie-Laurence Tremblay1, Lingling Xu2, Muzaddid Sarker3

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Spider wrapping silk proteins (W units) show distinct dynamics between folded cores and disordered linkers. This difference in protein dynamics is key to understanding how silk fibers form.

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aciniform spidroin (AcSp1)hydrodynamics characterizationmodular proteinsnuclear magnetic resonance spectroscopyrecombinant spider silkreduced spectral density mappingsegmental-labellingsplit inteinwrapping silk

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Area of Science:

  • Biomaterials Science
  • Protein Dynamics
  • Structural Biology

Background:

  • Spider aciniform silk is a biomaterial known for its exceptional mechanical properties.
  • This silk is composed of modular proteins, termed W units, which feature a globular folded core and disordered tails/linkers.

Purpose of the Study:

  • To characterize the backbone dynamics of single (W₁) and two-unit (W₂) spider silk proteins.
  • To investigate the role of protein dynamics in the fibrillogenesis of spider silk.

Main Methods:

  • Utilized nuclear magnetic resonance (NMR) spectroscopy, specifically (15)N spin relaxation analysis, to probe ps-ns timescale dynamics.
  • Employed segmental NMR isotope enrichment via split intein-mediated trans-splicing for unambiguous backbone dynamics mapping in W₂.

Main Results:

  • Revealed significant differences in dynamics between the folded core and the intrinsically disordered linker/tail regions of W units.
  • Observed that globular domains tumble nearly independently, suggesting modular behavior.
  • Identified elevated high-frequency dynamics in helix 5 compared to helix 4, supporting its role in unfolding during fiber formation.

Conclusions:

  • The distinct dynamics of folded and disordered regions are crucial for spider silk's unique properties and formation.
  • Helix 5's dynamics suggest a specific mechanism for unfolding during the transition to a β-sheet-rich fiber structure.