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Lecture

Protein Modifcation

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Department
Biochemistry
Course
Biochemistry 2280A
Professor
Eric Ball
Semester
Fall

Description
Protein ModificationProteins can be modified in a lot of ways that expand their different functionality Glycoproteincarbohydrate moteyattached to the protein It is within a lipid membrane protein with carbs sticking out the end Proteins are an incredibly diverse population by sequences then when you add phosphates you get a diversity of functionality Protein structures are held together purely by weak interactionshydrogen bonds electrostatic interactions van der Waals packing and hydrophobic interactions A single weak interaction contributes very little to the stability of a protein structure yet the very large number of these interactions act together cooperatively to impart high stability to the protein fold Cooperativity in a folding process demonstrates that the stability of the folded state is greater than the sum of the energies of the weak interactions involvedFolded proteins usually have a hydrophobic core in which side chain packing stabilizes the folded state and charged or polar side chains occupy the solventexposed surface where they interact with surrounding water Minimizing the number of hydrophobic sidechains exposed to water is an important driving force behind the folding process6 Formation of intramolecular hydrogen bonds provides another important contribution to protein stability The strength of hydrogen bonds depends on their environment thus Hbonds enveloped in a hydrophobic core contribute more than Hbonds exposed to the a
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