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lolocola03 lolocola03
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2 years ago
Hello Biology-forums community,

I'm currently studying the process of liquid-liquid phase separation as one of the proteins we study has been localized in membrane-less organelles.

I'm struggling to find a good explanation of how some amino acids (mainly polar, charged, arginine for example, lysine,...) can allow a protein to be flexible by forming intrinsically disordered regions. And how hydrophobic and aromatic ones drive a strict 3D structure...

I guess I don't understand how charges and hydropathy influence the structure of the protein. Would any of you be able to enlighten me or give me good recommendations?

Thank you in advance!

Good morning/evening,
A biomedical student with limitations regarding pure chemistry/biochemistry.
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Staff Member
2 years ago Edited: 2 years ago, bio_man
Hello, lolocola03

I've found a source for you to help you understand your problem a little better. See the attachment, and specifically start reading the segment Conformational states of intrinsically disordered regions.

Furthermore, I found a helpful excerpt on Wikipedia. It's provided for reference, but the link is shared below:

In general, IDPs are characterized by a low content of bulky hydrophobic amino acids and a high proportion of polar and charged amino acids, usually referred to as low hydrophobicity... [H]igh net charges promote disorder because of electrostatic repulsion resulting from equally charged residues... Many disordered proteins reveal regions without any regular secondary structure. These regions can be termed as flexible, compared to structured loops.

If you still need a better response, don't hesitate to respond back.
Source  https://en.wikipedia.org/wiki/Intrinsically_disordered_proteins
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