Protein structure: evolutionary bridges to new folds

Todd O Yeates1

  • 1UCLA Department of Chemistry and Biochemistry, 611 Charles Young Drive East, Los Angeles, California 90095-1569, USA. yeates@mbi.ucla.edu

Current Biology : CB
|January 24, 2007
PubMed
Summary

Novel protein folds may evolve from existing structures, crucial for understanding protein evolution. Studies on Hydra proteins reveal evolutionary transitions between distinct protein structures.

Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
128.0K
Protein Folding01:25

Protein Folding

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...
11.6K
Protein and Protein Structure02:15

Protein and Protein Structure

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...
88.2K
What is Evolutionary History?02:35

What is Evolutionary History?

Scientists record evolutionary history by analyzing fossil, morphological, and genetic data. The fossil record documents the history of life on Earth and provides evidence for evolution. However, both fossil and living organisms offer evidence that outlines Earth’s evolutionary history.
43.6K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
The...
19.9K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

No description available
15.1K