Author: Sarah Kearns
Editors: David Mertz, Zuleirys Santana Rodriguez, and Scott Barolo
In a previous post, we discussed how proteins fold into unique shapes that allow them to perform their biological functions. Through many physical and chemical properties, like hydrogen bonding and hydrophobicity, proteins are able to fold correctly. However, proteins can fold improperly, and sometimes these malformed peptides aggregate, leading to diseases like Alzheimer’s.
How can we figure out when the folding process goes wrong? Can we use computers to figure out the folding/misfolding process and develop methods to prevent or undo the damage done by protein aggregates?
Continue reading “Computing Levinthal’s Paradox: Protein Folding, Part 2”
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