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Related Concept Videos

Protein Folding01:22

Protein Folding

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Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Switching of BJT01:22

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Switching behavior in Bipolar Junction Transistors (BJTs) is a fundamental aspect utilized in various electronic circuits, particularly for digital logic applications like switches and amplifiers. In a typical switching circuit, a BJT alternates between cut-off and saturation modes, corresponding to the "off" and "on" states, respectively, thus behaving like an ideal switch.
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Microfluidic Mixers for Studying Protein Folding
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A dramatic protein fold switch powers a bactericidal nanomachine.

Yao He1,2,3, Annie Si Cong Li4,3, Xiaoying Cai1,2,3

  • 1Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles (UCLA), Los Angeles, CA, USA.

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Protein fold switching is key for function. The F7 pyocin uses a dramatic structural change to kill bacteria, offering new ways to fight drug-resistant pathogens.

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Area of Science:

  • Structural biology
  • Microbiology
  • Biochemistry

Background:

  • Protein fold switching enables diverse biological functions.
  • Phage tail-like structures are complex nanomachines involved in bacterial infection.
  • Understanding these mechanisms is crucial for developing new antimicrobial strategies.

Purpose of the Study:

  • To investigate the structural dynamics of the F7 pyocin.
  • To elucidate the mechanism of bacterial cell surface binding and membrane penetration.
  • To explore the potential of fold-switching mechanisms for novel bacteriocin development.

Main Methods:

  • Cryogenic electron microscopy (cryo-EM) and tomography.
  • Site-directed mutagenesis.
  • AlphaFold protein structure prediction.

Main Results:

  • A 163-residue segment in F7 pyocin transitions from an α-helical coiled-coil to a β-prism structure upon cell surface binding.
  • This structural switch remodels the tail tip, ejects the tape measure protein, and drives membrane puncture.
  • Mutations destabilizing the β-prism conformation abolish bactericidal activity, indicating the transition's energy powers penetration.

Conclusions:

  • F7 pyocin utilizes an ATP-independent, massive fold switch for bacterial cell penetration.
  • This mechanism represents a novel bacterial warfare strategy.
  • Fold-switching offers potential for engineering bacteriocins against multidrug-resistant pathogens.