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Related Concept Videos

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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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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Amyloid Fibrils03:03

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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-protein Interfaces02:04

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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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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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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Polymorphic protein phase transitions driven by surface anisotropy.

Alessandro Strofaldi1, Michelle K Quinn1, Annela M Seddon2

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|January 7, 2023
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This summary is machine-generated.

Protein mutations enhance self-assembly into diverse condensed phases. Double mutations in human γD-crystallin (HGD) yield novel amorphous particles and crystals, offering insights into protein polymorphism and coarse-grained models.

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Area of Science:

  • Biophysics
  • Protein Science
  • Materials Science

Background:

  • Protein phase transitions are crucial for biological function and are influenced by mutations.
  • Human γD-crystallin (HGD) mutants are linked to juvenile cataract and serve as models for protein assembly.
  • Understanding protein interactions guides the development of coarse-grained models.

Purpose of the Study:

  • To investigate how introducing new inter-protein interactions via mutagenesis affects protein self-assembly.
  • To characterize the condensed phases formed by a specific HGD double-mutant (P23VC110M).
  • To identify and describe novel amorphous protein particles.

Main Methods:

  • Site-directed mutagenesis to create HGD double-mutants.
  • Observation and characterization of protein self-assembly and phase transitions.
  • Microscopy and solubility studies to analyze particle morphology and properties.

Main Results:

  • Mutagenesis additively increases the number and variety of protein condensed phases.
  • The HGD double-mutant P23VC110M forms spherical particles, orthorhombic and needle/plate crystals, and undergoes liquid-liquid phase separation.
  • A novel, temperature-reversible amorphous protein particle formed by homogeneous nucleation was identified.

Conclusions:

  • Protein mutations can lead to complex and predictable polymorphic behavior.
  • The observed polymorphism is not fully predictable from single-mutant properties.
  • This study provides valuable data for refining coarse-grained models of protein assembly and phase transitions.