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Protein and Protein Structure02:15

Protein and Protein Structure

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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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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 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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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Protein Organization01:24

Protein Organization

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Sucralose Destabilization of Protein Structure.

Lee Chen1, Nimesh Shukla1, Inha Cho1

  • 1†Department of Physics, Wesleyan University, 265 Church Street, Middletown, Connecticut 06459, United States.

The Journal of Physical Chemistry Letters
|August 12, 2015
PubMed
Summary
This summary is machine-generated.

Artificial sweetener sucralose destabilizes protein structures, unlike sucrose. This effect is linked to sucralose's high polarity, impacting protein melting points and molecular dynamics.

Keywords:
Stokes−Einstein−Debye diffusioncircular dichroismdisaccharidefractional Stokes−Einstein−Debyeheterogeneous diffusionprotein stabilityrotational correlation timerotational diffusionsucralosesucrosetime-resolved fluorescence anisotropy

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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Molecular Biophysics

Background:

  • Sucralose, an artificial sweetener, differs significantly from sucrose in biomolecular interactions.
  • Understanding these differences is crucial for applications involving proteins and sweeteners.

Purpose of the Study:

  • To investigate the impact of sucralose on protein structure and dynamics.
  • To elucidate the biophysical mechanisms behind sucralose-protein interactions.
  • To compare sucralose's effects with those of sucrose.

Main Methods:

  • Studied the effect of varying sucralose concentrations on the melting temperature of bovine serum albumin and staphylococcal nuclease.
  • Utilized time-resolved fluorescence anisotropy to measure the dielectric friction and rotational diffusion of tryptophan.
  • Analyzed tryptophan diffusion in relation to bulk viscosity in both sucrose and sucralose solutions.

Main Results:

  • Sucralose linearly decreased the melting temperature of both model proteins.
  • Increased molecular polarity of sucralose was correlated with protein destabilization.
  • Tryptophan's rotational diffusion in sucralose solutions diverged from viscosity predictions, indicating heterogeneous diffusion.

Conclusions:

  • Sucralose acts as a protein destabilizer, unlike sucrose.
  • The high polarity of sucralose is a key factor in its interaction with biomolecules.
  • Sucralose induces non-Stokes-Einstein behavior in protein rotational diffusion.