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Related Concept Videos

Protein Denaturation01:28

Protein Denaturation

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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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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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Mechanistic elements of protein cold denaturation.

Carlos F Lopez1, Richard K Darst, Peter J Rossky

  • 1Center for Computational Molecular Sciences, Institute for Computational Engineering and Science, and Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, Texas 78712-1167, USA.

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Cold denaturation destabilizes globular proteins. Lower temperatures increase water-protein interactions, causing surface defects and disrupting protein structure, as observed in apomyoglobin simulations.

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Published on: March 4, 2017

Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Chemistry

Background:

  • Proteins can denature (lose structure) due to environmental changes.
  • Cold denaturation, a decrease in temperature causing unfolding, is counterintuitive.
  • Existing theories link cold denaturation to altered water-protein interactions and hydrophobic effects.

Purpose of the Study:

  • To investigate the molecular mechanisms of cold denaturation.
  • To analyze changes in protein hydration and local motions during cold denaturation.
  • To explore how temperature affects apomyoglobin structure and dynamics.

Main Methods:

  • Molecular dynamics simulations of apomyoglobin.
  • Simulations performed at 310 K and then cooled to 278 K.
  • Analysis of protein hydration, atomic fluctuations, and isothermal compressibility.

Main Results:

  • Increased solvent contacts around the protein, especially nonpolar atoms, at lower temperatures.
  • Enhanced atomic fluctuations and increased isothermal compressibility in protein core regions.
  • Evidence of solvent-induced packing defects at the protein surface.

Conclusions:

  • Lower temperatures promote favorable water-protein interactions, destabilizing protein structure.
  • Increased protein compressibility and atomic motion contribute to cold denaturation.
  • The study provides mechanistic insights into cold denaturation via molecular simulations.