Why do fibrous proteins more stable -according to Axial ratio- than globular ones although the bonds of globular seem to be at the central core of globular sub units .. while the fibrous sub units the bonds seem to be easily exposed to hydrolysis
Fibrous proteins generally have no tertiary structure to denature which makes them quite stable as far as structure goes. They also have many nonpolar residues on their surface which makes them less soluble in water than many globular proteins. Fibrous proteins often have repeating units of glycine or proline making some segments quite hydrophobic. They also have very few folding domains that would allow them to change shape under normal conditions. Globular proteins have many folding domains and relatively delicate bonds that are holding the shape of the protein which can result in conformation changes with slight environmental fluctuations. This is often a functional part of the protein to change shape when the environment changes state or one or more electronic changes happen in a specific region.
@Ron Reiserer
Thanks a lot. You have convinced me with the answer and added a lot of information to my knowledge. I really appreciate that, professor
Nadien Khaled Fahim Also the extensive hydrogen bonding in fibrous proteins make them achieve more stability, On the other hand there is lot of bending & twisting in globular proteins. These factors are dominant over the Axial Ratio.
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