Related Experiment Video
Updated: Jul 9, 2026

09:37
An Integrated Approach for Microprotein Identification and Sequence Analysis
Published on: July 12, 2022
Characters of very ancient proteins
Bin-Guang Ma1, Lei Chen, Hong-Fang Ji
1Shandong Provincial Research Center for Bioinformatic Engineering and Technique, Center for Advanced Study, Shandong University of Technology, Zibo 255049, PR China.
Biochemical and Biophysical Research Communications
|December 13, 2007
Summary
Ancient proteins
Area of Science:
- Origin of Life Research
- Protein Evolution
- Biochemistry
Background:
- Studying ancient proteins is crucial for understanding life's origins.
- Direct evidence is absent, necessitating indirect methods like molecular fossils.
Purpose of the Study:
- To outline prior findings on ancient protein characterization.
- To propose a new strategy for tracing ancient protein features.
- To identify common characteristics of very ancient proteins.
Main Methods:
- Analysis of molecular fossils within modern proteins.
- Utilizing diverse protein datasets.
- Comparative analysis of protein folds and functions.
Main Results:
- Identified six key protein folds common in ancient proteins: P-loop triphosphate hydrolases, TIM beta/alpha-barrel, NAD(P)-binding Rossmann-fold, Ferredoxin-like, Flavodoxin-like, and Ribonuclease H-like motif.
- Ancient protein functions are linked to purine, pyrimidine, porphyrin, chlorophyll, and carbohydrate metabolism.
- Some ancient proteins require cofactors like ATP, NADH, or NADPH.
Conclusions:
- Molecular fossils and protein datasets converge on similar conclusions about ancient protein characteristics.
- Ancient proteins likely possessed specific structural folds and metabolic functions.
- Cofactor dependency was a feature of some early proteins.
Related Concept Videos
Conservation of Protein Domains Over Different Proteins
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.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
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...
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...
Conserved Binding Sites
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Protein Organization
Overview
Protein Organization
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.

