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Related Concept Videos

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.
A protein's shape is critical to its function. For example, an enzyme...
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Protein Families02:47

Protein Families

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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
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Mechanical Protein Functions01:58

Mechanical Protein Functions

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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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Group Design02:01

Group Design

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The most basic experimental design involves two groups: the experimental group and the control group. The two groups are designed to be the same except for one difference— experimental manipulation. The experimental group gets the experimental manipulation—that is, the treatment or variable being tested—and the control group does not. Since experimental manipulation is the only difference between the experimental and control groups, we can be sure that any differences between...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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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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Designability of α-Helical Protein Filaments.

Abhinaba Das1, Vincent Conticello2

  • 1Department of Chemistry, Emory University, Atlanta, Georgia.

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This review explores protein helix-helix interactions for designing self-assembling nanomaterials. It highlights cross-alpha helical filaments and their potential for creating novel synthetic protein structures.

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Area of Science:

  • Protein structure and biophysics
  • Nanomaterials science
  • Computational biology

Background:

  • Helix-helix interactions are crucial for protein structure and assembly.
  • Naturally occurring alpha-helical protein filaments exhibit regular, designable interfaces.
  • These principles offer a foundation for de novo design of synthetic protein assemblies.

Purpose of the Study:

  • To review current knowledge of helix-helix interactions in natural protein filaments.
  • To discuss the implications for designing synthetic filamentous nanomaterials.
  • To evaluate the designability of cross-alpha helical filaments.

Main Methods:

  • Literature review of protein structure and assembly.
  • Analysis of naturally occurring alpha-helical protein filaments.
  • Case study on cross-alpha helical filaments, including PDB analysis and sequence-based prediction.

Main Results:

  • Helix-helix interactions provide designable interfaces for self-assembly.
  • Cross-alpha helical filaments, with perpendicular protomer orientation, represent a promising class.
  • The study evaluates the prevalence of cross-alpha interfaces and prediction accuracy.

Conclusions:

  • Understanding natural helix-helix interactions is key to designing synthetic protein nanomaterials.
  • Cross-alpha helical filaments offer significant potential for de novo design.
  • Further research can optimize the design of interfaces for specific self-assembled structures.