Related Experiment Video
Updated: Jul 13, 2026

Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D
Published on: May 19, 2018
The N-terminal domain of elastin-binding protein of Staphylococcus aureus changes its secondary structure in a
Makoto Nakakido1, Yoshikazu Tanaka, Kouhei Tsumoto
1Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan.
Abstract:
Elastin-binding protein of Staphylococcus aureus (EbpS) has been identified as an adhesin that can bind to soluble elastin or tropoelastin. However, the structure and exact function of EbpS remain to be elucidated. To gain insight into the molecular characteristics of EbpS, we investigated the physical properties of its N-terminal extracellular domain in various environments. CD spectroscopy showed that this protein was soluble and unstructured under aqueous conditions. Non-native secondary structures, however, were induced by several alcohols that provided membrane-mimetic environments. These changes may have some correlation with the function of this protein.
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Elastin is Responsible for Tissue Elasticity
Ligaments and tendons are made of dense regular connective tissue, but in ligaments not all fibers are parallel. Dense regular elastic tissue contains elastin fibers and...
Bacterial Protein Maturation
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Tail-anchoring of Proteins in the ER Membrane

