Final answer:
Basic Fibroblast Growth Factor binds to glycosaminoglycans and would likely be abundant in basic amino acids such as lysine, arginine, and histidine. These interact with the negatively charged molecules in the extracellular matrix. Soluble proteins have polar surfaces and hydrophobic interiors, while membrane proteins also accommodate hydrophobic amino acids in lipid bilayers.
Step-by-step explanation:
Basic Fibroblast Growth Factor (bFGF) binds to glycosaminoglycans (GAGs) in the extracellular matrix. The amino acids that would be abundant in bFGF, considering its interaction with these negatively charged molecules are basic amino acids. Basic amino acids, like lysine, arginine, and histidine, have a positive charge at physiological pH and can form ionic bonds with the negatively charged GAGs.
In general, soluble proteins typically have hydrophilic or polar amino acids on their surface to interact with the aqueous environment, while hydrophobic amino acids are located in the interior, away from water. Proteins embedded in lipid bilayers usually have hydrophobic amino acids in contact with the lipid's fatty acid chains and polar amino acids facing the aqueous environment. Additionally, in the case of the extracellular matrix, cells like fibroblasts produce large amounts of proteins such as collagen fibers, reticular fibers, and elastin fibers, contributing to the structure and function of connective tissues.