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Structural Protein Function01:56

Structural Protein Function

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
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The Sarcomere01:08

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A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
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Tension Response at Adherens Junctions01:26

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The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
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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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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
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Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

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[Changes in Titin Structure during Its Aggregation].

A G Bobylev1,2, E I Yakupova1, L G Bobyleva1

  • 1Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.

Molekuliarnaia Biologiia
|August 18, 2020
PubMed
Summary

Muscle titin protein forms unique amyloid-like aggregates in vitro. These aggregates exhibit a cross-β quaternary structure without altering secondary structure, differing from typical amyloid fibrils.

Keywords:
X-ray diffractionamyloid-like aggregatescross-β structurefunctional amyloidstitin

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Aggregation

Background:

  • Titin is a large muscle protein crucial for muscle elasticity.
  • Amyloid proteins form characteristic fibrillar aggregates with cross-β structures.
  • Understanding protein aggregation is vital for disease research and biomaterial development.

Purpose of the Study:

  • To investigate the in vitro aggregation properties of the muscle titin protein.
  • To characterize the structural features of titin aggregates and compare them to known amyloid structures.
  • To propose a model for the structural changes in titin during amyloid-like aggregate formation.

Main Methods:

  • In vitro protein aggregation assays.
  • X-ray diffraction analysis of titin aggregates.
  • Spectroscopic methods to assess secondary structure changes.

Main Results:

  • Titin forms specific amyloid-like aggregates in vitro.
  • These aggregates possess a quaternary structure resembling cross-β without changes in secondary structure.
  • X-ray diffraction data indicate parallel, not perpendicular, orientation of β-strands relative to the fibril axis.
  • Variable β-sheet spacing and orientation result in diffuse X-ray reflections (~8-12 Å).

Conclusions:

  • Titin aggregates are distinct from classical amyloid fibrils and should be termed 'amyloid-like'.
  • The unique quaternary structure arises from parallel β-strand arrangements and potentially partial domain unfolding.
  • These findings offer insights into novel protein aggregation mechanisms and structural diversity.