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CAS BI 315 (110)
Lecture 3

Lecture 3 BI315.docx

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Department
Biology
Course
CAS BI 315
Professor
Eric Widmaier
Semester
Spring

Description
Lecture 3 02/16/2014 Quaternary structure of proteins: multiple subunits (tertiary structures) put together. Not all proteins have  quaternary structures.  No protein storage; you can use amino acids for energy storage or use for energy but it is not a good thing;  take an amino acid and turn it into glucose: remove the amino group, rearrange into a glucose molecule in  the liver. This mechanism is controlled by insulin, nervous system and other hormones.  When energy is plenty: protein synthesis and glycogen synthesis (controlled by hormones, nervous system  and insulin) 4 hormones that break down (opposite of insulin) Cortisol­adrenal; steroid, anti­inflammatory­puts a break on the immune system.  Epinephrine­adrenal (adrenaline) Growth Hormones­Pituitary Glucagon­Pancreas (when glucose is gone)  Protein and ligand (binding sites): attractive with electrostatic forces to bind; also specificity; good/bad? Can  be both. Ligands that are not specific can bind to other proteins causing side effects because of other  protein interactions. Prednisone­stop the immune system for a short period of time; binds steroid receptors better then cortisol  and lasts longer and it depends on the kidneys.  Affinity of the receptor:  high affinity­don’t need much of the ligand. Intermediate affinity­ Low affinity; need a higher dose; higher the dose the more
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