Related Experiment Video
Updated: Jan 4, 2026
06:50
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
Published on: January 26, 2024
2.4K
FoldamerDB: a database of peptidic foldamers
Bilal Nizami1, Dorottya Bereczki-Szakál2, Nikolett Varró2
1MTA TTK Lendület Biomolecular Self-Assembly Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, H-1117 Budapest, Magyar Tudósok krt. 2, Hungary.
Nucleic Acids Research
|November 6, 2019
Summary
FoldamerDB is a new open-source database for peptidic foldamers, offering comprehensive information on their sequences, structures, and activities. This resource aims to support diverse scientific research in chemistry and biology.
Area of Science:
- Biochemistry
- Medicinal Chemistry
- Materials Science
Background:
- Foldamers are synthetic oligomers mimicking natural biomolecules, with significant therapeutic and material applications.
- Despite their potential, a centralized, accessible resource for foldamer information is lacking.
Purpose of the Study:
- To introduce FoldamerDB, a novel, curated, and open-source database for peptidic foldamers.
- To provide a comprehensive repository of foldamer sequences, structures, and biological activities.
Main Methods:
- Manual curation and annotation of foldamer data from over 160 research papers.
- Development of a user-friendly, searchable, and filterable web interface compatible with various devices.
Main Results:
- FoldamerDB contains information on 1319 foldamer species and 1018 activities.
- The database features a clutter-free, intuitive web interface for easy data exploration.
Conclusions:
- FoldamerDB addresses the need for a freely available, comprehensive resource on foldamers.
- The database is expected to benefit researchers across chemistry, biology, and related fields.
Related Concept Videos
02:47Protein Families
16.6K
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...
16.6K
01:22Protein Folding
125.7K
Overview
125.7K
01:25Protein Folding
10.8K
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...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
10.8K
02:21Globular and Fibrous Proteins
46.6K
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 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...
46.6K
01:24Protein Organization
8.9K
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.
The primary structure of a protein is its amino acid sequence....
The primary structure of a protein is its amino acid sequence....
8.9K
01:29Protein Folding Quality Check in the RER
4.9K
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...
4.9K