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The compacting factor test is a method used to assess the workability of concrete. It is  especially suitable for concrete mixes containing aggregates up to one and a half inches in size. This test involves specialized equipment consisting of two truncated cone-shaped hoppers and a cylinder, all with polished interior surfaces to minimize friction.
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Order, Disorder, and Temperature-Driven Compaction in a Designed Elastin Protein.

Kelly N Greenland1, Ma Faye Charmagne A Carvajal2, Jonathan M Preston1

  • 1Department of Physics , The City College of New York , New York , New York 10031 , United States.

The Journal of Physical Chemistry. B
|February 21, 2018
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Summary
This summary is machine-generated.

Artificial elastin miniconstructs reveal insights into protein structure and dynamics. These elastin-like proteins exhibit temperature-driven volume constriction, a novel structural change linked to their biological functions.

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Area of Science:

  • Biophysics
  • Protein Chemistry
  • Structural Biology

Background:

  • Natural elastin provides elasticity to tissues but is challenging to study.
  • Artificial minielastin constructs offer a simplified model for detailed structural analysis.
  • Understanding elastin structure is key to its biological functions like elastic recoil.

Purpose of the Study:

  • To investigate the structure and dynamics of elastin-like proteins using artificial minielastin constructs.
  • To achieve complete residue-specific resolution of elastin structure and dynamics via NMR.
  • To elucidate the temperature-dependent conformational changes in elastin domains.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy for residue-specific analysis.
  • Circular Dichroism (CD) spectroscopy to assess secondary structure.
  • Design and synthesis of artificial minielastin constructs.

Main Results:

  • Alanine-rich cross-linking domains show partial helical structure when adjacent to proline-rich hydrophobic domains.
  • Hydrophobic domains (VPGVGG, APGVGV repeats) appear as random coil but possess a dynamically disordered structural bias.
  • Elastin domains maintain a condensed conformation and exhibit significant temperature-driven volume constriction (up to 30%) without increased ordering.

Conclusions:

  • Artificial minielastin provides a powerful tool for studying elastin structure and dynamics.
  • Temperature-driven constriction is a novel protein structural change linked to elastin's coacervation and elastic recoil functions.
  • The findings offer new perspectives on intrinsically disordered protein behavior and nonbiological polymer-like properties in proteins.