Beruflich Dokumente
Kultur Dokumente
Amino Acids ➢ Among all possible amino acids, only 20 are usually found in
proteins
ENGR. JEREMI AH EMI ER VI L L AN U EVA ➢ All 20 naturally occurring amino acids in pure form are white,
CHEMI CAL ENGI NEERI NG DEPARTMEN T crystalline, high-melting solids.
ADAMSON U NI VERSI TY
➢ Protein structure and function is defined by the sequence and type ➢ At physiological pH (~7.4), amino acids exist as
of amino acids. zwitterions – positive and negative charge on
the same molecule. Dependent on the pKa of
the group.
1
2/6/2019
Stereochemistry Stereochemistry
➢ Every compound has a mirror image ➢ Superimposable mirror images: ACHIRAL
➢ Sometimes mirror images of a molecule are superimposable in ➢ Examples: two plain mugs, you can turn the
space with the original object. mirror image of the plain mug in space to make
➢ Non-superimposable mirror images: CHIRAL it superimposable.
➢ Greek word cheir: “hand”
➢ Have no plane of symmetry
➢ General rule: Carbon atom with 4 different atoms or groups
bonded to it.
➢ Example: hand or foot
Enantiomers Enantiomers
➢ Non-superimposable mirror images ➢ Each amino acid except glycine has
2 enantiomers.
➢ Most amino acids (except glycine) have four different groups
attached to the a-carbon. Chiral center. ➢ The enantiomers are classified
based on the ability to rotate
➢ Glycine – R is hydrogen. Therefore the mirror images ARE polarized light – optically active.
superimposable and NOT chiral. Also a plane of symmetry exists. ➢ Rotate light in either (+) or (-)
direction.
➢ Called D or L enantiomers.
➢ Racemic mixture – optically
inactive
2
2/6/2019
Enantiomers Examples
➢ Both D and L amino acids exist in ➢ Different flavors tasted depending
nature but only L amino acids are on the chirality of one carbon in
used as building blocks for proteins. carvone.
➢ D-amino acids are found in a few ➢ (+) spearmint
rare bacteria in the cell walls. ➢ (-) caraway
➢ Taste receptors can tell the
difference in 3-D structure of small
molecules.
➢ Taste buds are chiral environment.
3
2/6/2019
4
2/6/2019
Group 2: Neutral Polar Side chains Group 2: Neutral Polar Side chains
➢ Polar residues are also buried on the surface of proteins. ➢ Serine (S, Ser) and Threonine (T,
Thr)
➢ They form H-bonds with other polar residues in the protein or with
water. ➢ Polarity contributed by the
hydroxyl group (-OH)
➢ Example: Serine can both donate as well as accept a hydrogen ➢ Sugars attach to Ser and Thr to
bond. form glycoproteins
➢ Ser and Thr can have
phosphates attached – regulates
the activity of some proteins.
5
2/6/2019
Group 2: Neutral Polar Side chains Group 2: Neutral Polar Side chains
➢ Tyrosine (Y, Tyr) ➢ Adrenaline
➢ Fluorescent – absorbs UV light ➢ “fight or flight” hormone
at 280 nm (easy to identify) ➢ causes release of glucose and
➢ Can be phosphorylated (have other nutrients into the blood
phosphates attached) and stimulates brain function
➢ Derived from phenylalanine
➢ Converted to catecholamines –
includes epinephrine
(adrenaline)
Group 2: Neutral Polar Side chains Group 2: Neutral Polar Side chains
➢ Asparagine (N, Asn) and ➢ Cysteine (C, Cys)
Glutamine (Q, Gln) ➢ Sulfhydryl side chain (-SH)
➢ Classified as amides which gives polarity.
➢ Neither acidic nor basic ➢ Can oxidize to form disulfide
➢ Forms H-bonds bonds that strengthen protein
➢ Asn can be modified with structure
sugars to form glycoproteins ➢ Disulfide bonds are covalent
but reversible upon reduction
6
2/6/2019