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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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.
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Protein Folding01:25

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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.
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Protein and Protein Structure02:15

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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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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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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
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Microfluidic Mixers for Studying Protein Folding
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Heterogeneity in Protein Folding and Unfolding Reactions.

Sandhya Bhatia1,2, Jayant B Udgaonkar1,2

  • 1National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bengaluru 560065, India.

Chemical Reviews
|March 11, 2022
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Summary

Understanding protein dynamics is key to protein folding. Researchers are resolving conformational heterogeneity in proteins, revealing complex folding pathways and energy landscapes.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Dynamics

Background:

  • Proteins exhibit dynamic structures with motions across diverse timescales.
  • Conformational heterogeneity is crucial for understanding protein folding mechanisms.
  • Previous studies highlight the importance of resolving protein dynamics.

Purpose of the Study:

  • To investigate and resolve site-specific conformational heterogeneity during protein folding.
  • To elucidate the mechanistic aspects of protein folding reactions.
  • To understand the origins and implications of conformational heterogeneity.

Main Methods:

  • Utilizing high-resolution structural probes sensitive to population distributions.
  • Analyzing conformational heterogeneity across different protein states (unfolded, intermediate, native).
  • Investigating the role of physicochemical interactions and protein-solvent interactions.

Main Results:

  • Significant conformational heterogeneity observed in unfolded, intermediate, and native protein states.
  • Heterogeneity arises from reduced cooperativity of interactions and potential functional/evolutionary constraints.
  • Conformational substates and slower exchange rates contribute to heterogeneity in folding pathways.

Conclusions:

  • Resolving protein conformational heterogeneity provides critical insights into folding pathways and energy landscapes.
  • Understanding heterogeneity is essential for accurate mechanistic understanding of protein folding and unfolding.
  • This research highlights the complex nature of protein dynamics and conformational landscapes.