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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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In most main group element compounds, the valence electrons of the isolated atoms combine to form chemical bonds that satisfy the octet rule. For instance, the four valence electrons of carbon overlap with electrons from four hydrogen atoms to form CH4. The one valence electron leaves sodium and adds to the seven valence electrons of chlorine to form the ionic formula unit NaCl (Figure 1a). Transition metals do not normally bond in this fashion. They primarily form coordinate covalent bonds, a...
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Coordination Number and Geometry02:57

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For transition metal complexes, the coordination number determines the geometry around the central metal ion. Table 1 compares coordination numbers to molecular geometry. The most common structures of the complexes in coordination compounds are octahedral, tetrahedral, and square planar.
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The structure of a crystalline solid, whether a metal or not, is best described by considering its simplest repeating unit, which is referred to as its unit cell. The unit cell consists of lattice points that represent the locations of atoms or ions. The entire structure then consists of this unit cell repeating in three dimensions. The three different types of unit cells present in the cubic lattice are illustrated in Figure 1.
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Equations of Motion: Rectangular Coordinates and Cylindrical Coordinates01:21

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Understanding the motion of particles is a fundamental aspect of classical mechanics, and the choice of the coordinate system plays a pivotal role in unraveling the complexities of their dynamics.
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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An ultra-stable gold-coordinated protein cage displaying reversible assembly.

Ali D Malay1,2, Naoyuki Miyazaki3, Artur Biela4,5

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|May 10, 2019
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Researchers created a novel, ultra-stable artificial protein cage using metal coordination. This inducible protein assembly, controlled by gold or mercury ions, offers new possibilities for supramolecular chemistry and biomaterials.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Synthetic Biology

Background:

  • Protein cages are vital in nature for functions like compartmentalization and cargo delivery.
  • Designing controllable, inducible protein assemblies remains a significant challenge in synthetic biology.

Purpose of the Study:

  • To engineer an ultra-stable artificial protein cage with metal-controlled assembly and disassembly.
  • To explore novel supramolecular geometries and robust protein linking strategies.

Main Methods:

  • Utilized cysteine-substituted protein rings and gold(I)-triphenylphosphine compounds for self-assembly.
  • Employed cryo-electron microscopy to characterize the resulting supramolecular structures.
  • Investigated the role of metal coordination (gold and mercury) in cage formation.

Main Results:

  • Successfully generated monodisperse artificial protein cages exceeding 2 MDa, based on an unprecedented Archimedean snub cube geometry.
  • Confirmed the cage structure is stabilized by 120 S-Au(I)-S linkages and exhibits two chiral forms.
  • Demonstrated extreme chemical and thermal stability, with facile disassembly triggered by reducing agents.

Conclusions:

  • Established a method for creating robust, higher-order protein structures through metal-coordinated assembly.
  • Expanded the design possibilities for supramolecular assemblies with novel geometries.
  • Showcased the potential of metal-responsive protein cages for advanced applications.