“ CO-R-N ” clockwise When viewing down from H to C-alpha L-amino acid Proteins are built from 20 kinds of alpha-amino acids. 21 st aa = selenocysteine
Free -SH group of cysteine: -Reacts readily with heavy metals -Easily oxidized S S
pKa Three- and one-letter codes for amino acids
Insulin sequence Disulfide bond
Modified amino acid residues
Peptide unit: -Rigid -Usually trans -Dipole moment H Rotation around this C-N bond is not free.
These two bonds are free to rotate.
Alpha-helix has a large dipole moment
Antiparallel beta-sheet Collagen sequence Proteins: -Fibrous proteins eg. keratin, collagen, silk -Globular proteins
G, Gly Collagen triple helix
Myoglobin is rich in alpha-helices.
Ribonuclease: beta and alpha 4 disulfide bonds
Beta-alpha-beta motif: The crossover connection is nearly always right- handed. Hemoglobin: tetramer Poliovirus: 60-mer
Antibody light chain: beta-sandwich Ribonuclease sequence
Proteins can be easily denatured. Refolding of proteins is very difficult.
Conformational change is important for function.