Proteins: Structure and Function. Proteins. Cellular Overview Functions Key Properties Core Topics Amino Acids: properties, classifications, pI Primary Structure, Secondary Structure, and Motifs Tertiary Structure Fibrous vs. Globular Quaternary Structure. Amazing Proteins: Function.
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Proteins: Structure and Function
Thrombin and Fibrinogen
R-group or side-chain
20 common amino acids make up the multitude of proteins we know of
There are some important uncommon amino acids we shall still encounter later on.
Net charge: +1
Net charge: -1
Net charge: 0
Basic amino acids
Function as bases at physiological pH
Side chains with N
Acidic amino acids
Negatively charged at physiological pH
Side chains with –COOH
Predominantly in unprotonated form
We use different “levels” to fully describe the structure of a protein.
– Amino acids that favor α helices:
Glu, Gln, Met, Ala, Leu
– Amino acids that disrupt α helices:
Val, Thr, Ile, Ser, Asx, Pro
Modeling protein folding with Linus (George Rose)
An amphiphilic helix in flavodoxin:
A nonpolar helix in citrate synthase:
A polar helix in calmodulin:
ADVANTAGES of 4o Structures