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Related Concept Videos

Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Families02:47

Protein Families

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 locations, protein...

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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
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Published on: March 10, 2021

Foldamers with heterogeneous backbones.

W Seth Horne1, Samuel H Gellman

  • 1Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.

Accounts of Chemical Research
|July 2, 2008
PubMed
Summary
This summary is machine-generated.

Chemists are designing synthetic foldamers with mixed alpha- and beta-amino acid backbones. These heterogeneous foldamers mimic biopolymers, showing promise for antimicrobial agents and inhibiting protein-protein interactions in biomedical applications.

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Published on: November 3, 2011

Area of Science:

  • Synthetic chemistry
  • Biochemistry
  • Materials science

Background:

  • Proteins and nucleic acids are essential for life.
  • Synthetic oligomers are being developed to mimic biopolymer complexity.
  • Foldamers are non-natural oligomers with defined folding properties.

Purpose of the Study:

  • To explore the potential of heterogeneous backbone foldamers.
  • To highlight examples containing both alpha- and beta-amino acid residues.
  • To showcase advancements in alpha/beta-peptide foldamer design and applications.

Main Methods:

  • Designing and synthesizing heterogeneous backbone foldamers with alpha- and beta-amino acid residues.
  • Utilizing block strategies and interspersed monomer patterns for oligomer construction.
  • Employing crystallographic analysis to determine quaternary structures.

Main Results:

  • Demonstrated biopolymer-like conformational behavior in synthetic backbones.
  • Developed alpha/beta-peptide foldamers with novel helical secondary structures and quaternary arrangements.
  • Achieved biological functions, including antimicrobial activity and inhibition of protein-protein interactions.

Conclusions:

  • Heterogeneous backbone foldamers offer expanded structural and functional capabilities.
  • Alpha/beta-peptide foldamers show significant potential for biomedical applications.
  • Further research into foldamer design can lead to new therapeutic agents.