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Related Concept Videos

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
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Molecular Chaperones and Protein Folding03:00

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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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Gene Evolution - Fast or Slow?02:05

Gene Evolution - Fast or Slow?

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The genomes of eukaryotes are punctuated by long stretches of sequence which do not code for proteins or RNAs. Although some of these regions do contain crucial regulatory sequences, the vast majority of this DNA serves no known function. Typically, these regions of the genome are the ones in which the fastest change, in evolutionary terms, is observed, because there is typically little to no selection pressure acting on these regions to preserve their sequences.
In contrast, regions which code...
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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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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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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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Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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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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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

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Protein folding rate evolution upon mutations.

Jorge A Vila1

  • 1IMASL-CONICET, Universidad Nacional de San Luis, Ejército de Los Andes 950, 5700 San Luis, Argentina.

Biophysical Reviews
|September 8, 2023
PubMed
Summary
This summary is machine-generated.

Anfinsen's dogma ensures proteins fold quickly, regardless of sequence. This finding simplifies understanding protein evolution and how mutations impact protein evolvability.

Keywords:
Anfinsen dogmaEvolutionFolding rateLevinthal paradoxMutationsPost-translational modificationsProtein marginal stability

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Area of Science:

  • Structural Biology
  • Evolutionary Biology
  • Biophysics

Background:

  • Protein folding is essential for biological function, yet the speed at which proteins reach their native state remains a complex question.
  • Understanding protein folding dynamics is crucial for deciphering the impact of mutations and evolutionary processes on protein structure and function.

Purpose of the Study:

  • To investigate the fundamental principles governing the timescale of protein folding.
  • To explore the relationship between protein sequence, folding rate, and evolutionary adaptability.
  • To determine if protein folding evolution can be analyzed without considering epistasis or detailed mutational pathways.

Main Methods:

  • Analysis of Anfinsen's dogma in the context of protein folding kinetics.
  • Theoretical modeling to assess the feasibility of determining evolutionary changes in protein folding rates.

Main Results:

  • Anfinsen's dogma supports the rapid attainment of native protein states irrespective of sequence or length.
  • It is feasible to study the evolution of protein folding rates without accounting for epistasis or specific mutational trajectories.

Conclusions:

  • Protein folding speed is robust and predictable, supporting evolutionary biology and structural biology.
  • These findings provide a foundation for understanding mutation effects on protein evolvability and sequence-structure relationships.