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Related Concept Videos

Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
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Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
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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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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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Related Experiment Video

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Microdissection of Black Widow Spider Silk-producing Glands
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Mesoscale structures in amorphous silks from a spider's orb-web.

Christian Riekel1, Manfred Burghammer2, Martin Rosenthal2

  • 1The European Synchrotron, ESRF, CS40220, 38043, Grenoble Cedex 9, France. riekel@esrf.fr.

Scientific Reports
|October 24, 2020
PubMed
Summary
This summary is machine-generated.

Orb-web spiders use unique silk fibers for web construction. This study reveals distinct mesoscale structures in amorphous silk fibers, suggesting roles in enhancing web strength and cohesion.

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Area of Science:

  • Biomaterials Science
  • Materials Science
  • Structural Biology

Background:

  • Orb-web spiders utilize multiple silk types, but only major ampullate silk's structure and mechanics are well-understood.
  • Knowledge of mesoscale assembly (>50-100 nm) and its impact on mechanical properties of silks is limited.
  • The hierarchical organization of less crystalline silk fibers in orb-webs remains largely unexplored.

Purpose of the Study:

  • To investigate the mesoscale structural organization of two distinct amorphous silk fibers from an orb-web's center.
  • To elucidate the assembly mechanisms and potential functional roles of these less-studied silk fibers.
  • To compare the structural features of amorphous fibers with known silk types like major ampullate and egg case silks.

Main Methods:

  • Scanning X-ray micro&nanodiffraction was employed to analyze the mesoscale features of the silk fibers.
  • Detailed structural characterization at the micro and nanoscale was performed.
  • The interaction between different silk fiber types was examined.

Main Results:

  • Two fully amorphous silk fibers exhibited different mesoscale structures: one with a fibrillar composite structure, the other with a skin-core organization.
  • The skin-core fiber featured a nanofibrillar ribbon wound around a disordered core, with some nanofibrils forming mesoscale fibrils.
  • This fiber readily attached to the major ampullate silk's coat, detaching a glycoprotein skin-layer containing polyglycine II nanocrystallites.

Conclusions:

  • The distinct mesoscale architectures of amorphous silk fibers suggest specialized functions within the orb-web.
  • The observed attachment mechanism indicates a potential role for these fibers in reinforcing the tension and cohesion of major ampullate silk fibers.
  • Further research into the hierarchical organization of diverse silk types can reveal novel biomaterial properties and functions.