BSCI-1510 Lecture 3: Kendal Broadie- Protein Structure, Folding, and Function- August 29th, 2018

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Midterm 1, lecture 4: protein structure, folding, and function. Have an amino n- terminus (left side) and a carboxy c-terminus (right side) # of proteins that can be created is essentially unlimited. 20 aas (amino acids) and 20^n combinations and post translational modifications (aka covalently bonded addition of a group like -oh, acetyl, etc. or other proteins to the amino acid side chains) Primary (i) is linear sequence of amino acids with covalent peptide bonds in between. Secondary (ii) is the folding of the structure via h (hydrogen) bonds between backbone peptide bonds (h bonding occurs between h and o atoms on a protein) 2 types, which one depends of which is the most stable option (affected by. Stabilized by h bonds between n-h (peptide bond) and c=o (bond that is 4 aas away on the polypeptide) R side groups (aka aa side groups) radiate out from the helix.

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