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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.
The...
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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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Conservation of Protein Domains Over Different Proteins02:26

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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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Intrinsically Disordered Proteins02:18

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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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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The Unfolded Protein Response01:37

The Unfolded Protein Response

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Entropy-Enthalpy Compensations Fold Proteins in Precise Ways.

Jiacheng Li1, Chengyu Hou2, Xiaoliang Ma1

  • 1National Key Laboratory of Science and Technology on Advanced Composites in Special Environments, Center for Composite Materials and Structures, Harbin Institute of Technology, Harbin 150080, China.

International Journal of Molecular Sciences
|September 10, 2021
PubMed
Summary
This summary is machine-generated.

Protein folding is driven by entropy-enthalpy compensations, initiated by hydrophobic collapse of side-chains. This process guides the formation of secondary, tertiary, and quaternary structures through specific physical codes and forces.

Keywords:
H-bondsenthalpyentropyprotein-foldingthermodynamic

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Protein Folding

Background:

  • Intramolecular hydrogen bonds are crucial for protein structure stabilization.
  • Protein folding requires overcoming hydrogen bonding with water molecules, governed by entropy-enthalpy compensations.
  • The Gibbs free energy equation and enthalpy changes dictate these processes.

Purpose of the Study:

  • To elucidate a protein-folding mechanism based on entropy-enthalpy compensations.
  • To analyze the role of hydrophobic collapse in initiating protein folding.
  • To decipher the physical folding codes and forces within amino acid sequences.

Main Methods:

  • Analysis of spatial side-chain arrangements in experimentally determined protein structures.
  • Evaluation of hydrophobic interactions among neighboring side-chains in unfolded polypeptides.
  • Bioinformatics analysis of protein dimer structures.

Main Results:

  • A protein-folding mechanism initiated by laterally hydrophobic collapse of adjacent side-chains was revealed.
  • Hydrophobic collapse promotes intramolecular hydrogen bond formation via entropy-enthalpy compensation, enabling reproducible folding.
  • Folding codes for β-strands and α-helices were accurately deciphered by evaluating hydrophobic interactions.
  • Quaternary structure folding is guided by entropy-enthalpy compensations at subunit docking sites.

Conclusions:

  • Protein folding is a multistage process driven by entropy-enthalpy compensations between polypeptide chains and water molecules.
  • The temperature dependence of protein folding is linked to environmental influences on conformational Gibbs free energy.
  • The study provides a physical basis for understanding protein folding mechanisms.