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This interactive unit in Biochemistry 101 aims to deepen students' comprehension of the four fundamental forces in biochemistry: ionic bonds, hydrogen bonds, hydrophobic effects, and van der Waals interactions. The main objective is for students to leverage their knowledge to design a protein that can effectively bind to a specific peptide, considering the physical properties of amino acids. Following a series of lectures and discussions, students will engage in a hands-on protein design exercise inspired by Prof. Lynne Regan’s research, enhancing their practical understanding of protein interactions.
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OVERALL GOAL: • Students will understand the four forces of biochemistry (ionic bonds, H bonds, hydrophobic effect, van der Waals interaction) • OBJECTIVE: • Students will design a protein to bind a specific peptide by applying their knowledge of the four forces and the physical properties of different amino acids.
Example of a Friday discussion section that will be led by Postdoctoral Scholar - Students will have previously had 3 lectures covering the following topics: • What is Biochemistry? • Protein structure, primary through quaternary • Protein function and folding - Students will have had one homework assignment which reinforced different learning goals from the ones we are covering in this exercise.
Protein Design Based on Prof. Lynne Regan’s Research
Scaffold Ligand
? D3 ? F4 S2 ? R1 ?
Lys D3 F4 Trp S2 R1 Arg Asp