BCH210H1 Lecture Notes - Lecture 6: Protein Folding, Explosive Material, Phenylalanine

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos

Document Summary

It goes from a folded chain to a secondary structure which allows the tertiary structure to form. Phenylalanine needs to fit inside the pocket, and since it has a small chi angle, it can fold and fir in a s(cid:373)all po(cid:272)ket of the protei(cid:374). If it"s a residue that fa(cid:272)es the protei(cid:374) surfa(cid:272)e, the side (cid:272)hai(cid:374) (cid:272)a(cid:374) (cid:271)e very free to rotate because theres nothing in its way. The core of the protein is very well defined. The outside portions of the protein is very important for protein-protein interactions. If we change the primary sequence, we could change the secondary and tertiary structure. Proteins are(cid:374)"t very sta(cid:374)le, they (cid:272)a(cid:374) (cid:271)e very easily u(cid:374)folded. The same sequence can have different conformational states, and these different states have diferent functions. The disulfide link is formed in the er. Inside the lumen of the er, its an oxidizing environment allowing bonds to form.