Physicochemical properties

Amino acids Proteins Lipids

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Chemical structure & composition Chemical structure & composition Chemical structure & composition
Amino acids are organic compounds consisting of Proteins are polymers of amino acids. Generally, lipids are present as monomers of
amino (NH2) group, carboxyl (COOH) group, They are formed by peptide bonds between fatty acids & classified as
hydrogen atom, & a specific side chain (R group) amino acids. triglycerides/triacylglycerols (TAGs),
attached to central carbon atom. Peptide bond form between the carboxyl group phospholipids, sphingolipids, waxes, steroids,
2 of one amino acid and the amino group of eicosanoids, & isoprenoids.
Isoelectric point (pI) another amino acid. Lipids are generally composed of saturated or
At pH=pKa of an amino acid, it has net electric Primary structure of a protein is the sequence of unsaturated fatty acids with hydrophilic polar
charge of zero. amino acids. head group & hydrophobic non-polar tail.
An amino acid is positively charged if pH of the Secondary structure of a protein is the hydrogen 2
solution is below pKa of an amino acid. bonding based interactions in alpha helices & Melting point
An amino acid is negatively charged if pH of the beta sheets of a protein. Lipids that are composed of saturated fatty acids
solution is above pKa of an amino acid. Tertiary structure of a protein is the interaction with longer fatty acid chain have higher melting
3 of protein with its environment by ionic bonding, point than lipids that are composed of
Polarity & solubility hydrogen bonding, hydrophobic forces, disulfide unsaturated fatty acids.
Polar amino acids get dissolved in polar solvent, bonding, etc. 3
non-polar amino acids get dissolved in non-polar Quaternary structure of a protein is the Polarity & solubility
solvent, & charged amino acids interact interaction between subunits of a protein. Lipids composed of fatty acids have hydrophilic
accordingly with positive/negatively charged Some proteins are composed of non-amino acid (polar) carboxyl group and a hydrophobic
solvent. groups referred to as prosthetic groups, eg., (nonpolar) hydrocarbon tail.
4 heme group of hemoglobin; some proteins Due to amphipathic nature certain lipids form
Buffering capacity contain cofactors or coenzymes. miscelles, & phospholipids form bilayer as
The ionizable groups of an amino acid can donate 2 observed in cell membrane.
or accept protons at pH closer to its pKa, & acts Isoelectric point (pI) Lipids are soluble in non-polar hydrophobic
as buffer. At pH=pKa of a protein, it has net electric charge solvent.
5 of zero. 4
Absorption of UV light A protein is positively charged if pH of the Viscosity
Aromatic rings of tryptophan, tyrosine, & solution is below pKa of a protein. Fats (eg., butter) & waxes (eg., beeswax) have
phenylalanine absorb UV light & the amount of A protein is negatively charged if pH of the higher viscosity & are solid at room temperature
absorbed UV light is an indicator of protein's solution is above pKa of a protein. whereas oils (eg., sunflower oil) have lower
tertiary structure. 3 viscosity & are liquid at room temperature.
Polarity & solubility 5
Polarity is influenced by polar, non-polar, & Chemical reactivity
charged amino acids in protein. Oxidation of unsaturated fatty acids can happen
Polar amino acids are generally present on outer in lipids.
surface of protein & interacts with ligand, Hydrolysis of lipids, enzymatically by lipase,
substrate, & various components of its results in free fatty acids.
environment. 6
Non-polar amino acids are generally present on Absorption of UV light
inner surface of protein & is responsible for Lipids absorb UV light mainly due to unsaturated
hydrophobic interactions in protein. fatty acids & aromatic rings.
Solubility of a protein is influenced by polar, non- 7
polar, & charged amino acids in protein, Biological activity
concentration of protein, temperature, pH, & Lipids are present as energy reserve (TAGs),
composition of protein containing solution, selectively permeable membrane
chemical group/s introduced by post (phospholipids), participates in cell signalling
translational modification/s. (sphingolipids), waterproofing (waxes), acts as
4 hormones (steroids), involved in blood clotting
Thermal stability (eicosanoids), & functions as pigments
Proteins are classified as psychrophilic (active at (isoprenoids).
0-20°C), mesophilic (active at 20-45°C), or
thermophilic (active at 45-80°C) based on their
temperature connected catalytic activity.
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pH sensitivity
Proteins are classified as acidic (pI<7, eg.,
pepsin), basic (pI>7, eg., histones), or amphoteric
(can act as either acidic or basic depending on
the surrounding pH, eg., albumin) proteins.
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Absorption of UV light
Proteins absorb UV light due to aromatic amino
acids such as tryptophan (280 nm) & to a certain
extent tyrosine (275 nm) & phenylalanine (257
nm).
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Biological activity
Proteins act as enzymes, receptors, transporters,
antibodies, structural proteins, storage proteins,
etc.