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Lecture 3

Biochemistry 2280A Lecture Notes - Lecture 3: Equilibrium Constant, Ribosome, Proteasome

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Eric Ball

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Thursday, September 17, 2015
Protein Structure (2)
Meakin Lecture 4
By the end of today:
-define and describe tertiary and quaternary structure
-be able to describe a protein domain’s characteristics
-learn how proteins fold and how they become unfolded
-understand the concept of protein families
-be able to list different functions of proteins
-understand post-translational modifications
-understand what ligands are and how they bind to proteins
-understand the concept of Dissociation Constant (Kd)
3º Structure: Domains
-a critical concept for larger proteins
-definition: distinct region of a protein
domains can often fold independently
domains provide structure and/or function
-many proteins made up of connected domains
-related domains often found in different proteins
evolution has ‘mixed and matched’ domains
Quaternary Structure
-more than one protein!
-many proteins consist of more than one polypeptide
-these are called a protein’s subunits
-forces/bonds involved are the same as for 3º
hydrophobic, H-bonds, van der Waals, ionic,
disulfide bonds
- structure “coiled coil” —>
Examples of Proteins Containing Coiled Coils
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