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proteins
Properties of Amino Acids
• capacity to polymerize
• novel acid-base properties
• varied structure and
chemical functionality
• chirality
• D –amino acids are not found proteins but found in
nature.
• Crystalline amino acids are colorless, odorless, and
melt with decomposition at temperature more than 200
°C.
• The physical properties of amino acids are resemble
those of inorganic salt such as sodium chloride
• The name protein is giving to compounds containing
more than 100 amino acids. An amino acid unite in a
polypeptide or protein is called residue.
Functions of proteins
a-carbon is chiral
(except for glycine) amino group
at pH 7.0 uncharged
amino acids are
zwitterions
amino acids have a a-carbon
tetrahedral structure side chain
• Proteins are make about two third of dry weight of
cell.
• Major compounds of muscle, skin, and bones
• The molecular weight varied from several
thousand to several million.
• Treated with a boiled acids or bases solution
hydrolyzed the smaller compounds.
• Twenty amino acids are obtain from hydrolysis of
all living systems.
Amino Acid Enantiomers
•Steroisomers / enantiomers
•Biological system only
synthesize and use L-amino-
acids
Amino Acid Classification
• Aliphatic
• Aromatic Hydrophobic
• Sulfur containing
• Polar/uncharged
Hydrophillic
• basic/acidic
Aliphatic (alkane) Amino Acids
•Leucine (Leu, L) –
• Glutamate –
Basic Amino Acids
• Hydrophillic nitrogenous bases
• Positively charged at physiological pH
• Histidine – imidazole ring protonated/ionized, only amino
acid that functions as buffer in physiol range.
• Lysine - diamino acid, protonated at pH 7.0
• Arginine - guianidinium ion always protonated, most basic
amino acid
Polar Uncharged Amino Acids
• Polar side groups, hydrophillic in nature, can form hydrogen
bonds
Primary Assembly
STRUCTURE
PROCESS
Secondary Folding
Tertiary Packing
Quaternary Interaction
• Hydrogen bond is the responsible for secondary
structure.
• The attractive force in addition to hydrogen bond
between parts of proteins that important in
determining their shape.
• The α-amino acid coil as right handed screw
• The β-plated sheet structure are arranged side by
side and are hold together by hydrogen bond
between chains.
• The silk fibers is proteins that exist as a β-pleated
sheets