Amino Acids: !! What are amino acids? !! Structure of amino acids !! Classification of Amino acids !!

Essential & Non Essential Amino acids !! Disorder of Amino Acid Metabolism

Proteins
!! What are proteins? !! Types of Proteins !! Level of Protein Structures !! Formation of Proteins !! Protein Shape and Function !! Protein Synthesis !! Disorder of Proteins

!!An amino acid is one of the most importantly organic compounds containing both a functional carboxyl (-COOH) and an amino(-NH2) group. !!It is also accompanied by a side chain specific to each amino acid

The twenty naturally occurring amino acids that comprise proteins are (almost) ALL of the L- form. The L- (Laevorotatory) form is the stereoisomer that rotates plane polarized light to the left (I won't elaborate on this)

!!Amino acids are categorized into varies groups according to the charge polarity of the side chains. !!Nonpolar Side chains !!Uncharged Amino Acids !!Acidic Sides Chains !!Basic Side Chains

Each amino acid is shown in its fully protonated form, with dissociable hydrogen ions represented in red print.

! Dietary protein is the main source of amino acids. Amino acids * can be used as fuel, but usually more important roles for them are as building blocks for proteins, and as a source of carbon and nitrogen for biosynthesis of other biochemicals. ! In the process of digestion, proteins are broken down to free amino acids in the gastrointestinal tract. ! They are then absorbed and pass into the circulation, and are transported to liver where -NH2 groups are removed by transamination. The resulting alpha-keto acid is then used as fuel, or as a biosynthetic intermediate.
! !

Amino acids are not stored in the body like fats or carbohydrate; there are no specialized cells in the body to maintain a reservoir. Of course, amino acids are ubiquitous, being present in structural proteins, enzymes, transport proteins, etc.

! Some of these proteins (notably serum albumin) can be degraded under conditions of fasting or starvation, to release free amino acids.

Adult humans are unable to synthesize all twenty amino acids needed for protein synthesis; those which cannot be synthesized and which must then be acquired via the diet are referred to as essential. The ten which the body can synthesize on its own are nonessential. The ten essential amino acids for adults are:

!!At acidic pH, the carboxyl group is protonated and the amino acid is in the cationic form !!At neutral pH, the carboxyl group is deprotonated but the amino group is protonated. The net charge is zero; such ions are called Zwitterions !!At alkaline pH, the amino group is neutral NH2 and the amino acid is in the anionic form.

Histidine, an essential amino acid, has as a positively charged imidazole functional group. The imidazole makes it a common participant in enzyme catalyzed reactions. The unprotonated imidazole is nucleophilic and can serve as a general base, while the protonated form can serve as a general acid. The residue can also serve a role in stabilizing the folded structures of proteins

! MSUD is a metabolic disorder caused by a deficiency of the branched-chain alpha-keto acid dehydrogenase complex (BCKDC), leading to a build-up of the branched-chain amino acids (leucine,isoleucine,valine) and their toxic byproducts (ketoacids) in the blood and urine. ! The branched-chain !-ketoacid dehydrogenase complex (BCKDC) is a multisubunit complex of enzymes that is found on the mitochondrial inner membrane.

! The disease is named for the presence of sweet-smelling urine, with an odor similar to that of maple syrup. The smell is also present and sometimes stronger in the ear wax of an affected individual. ! From early infancy, symptoms of the condition include poor feeding, vomiting, dehydration, lethargy, hypotonia, seizures, hypoglycaemia, ketoacidosis, pancreatitis, coma and neurological decline ! A diet with minimal levels of the amino acids leucine, isoleucine, and valine must be maintained in order to prevent neurological damage.

! Most diverse and complex macromolecules in the cell ! Used for structure, function and information ! Made of linearly arranged amino acid residues. ! folded up with active regions

1) Enzymes catalyzes covalent bond breakage or formation 2) Structural collagen, elastin, keratin, etc. 3) Motility actin, myosin, tubulin, etc. 4) Regulatory bind to DNA to switch genes on or off 5) Storage ovalbumin, casein, etc. 6) Hormonal insulin, nerve growth factor (NGF), etc. 7) Receptors hormone and neurotransmitter receptors 8) Transport carries small molecules or irons 9) Special purpose proteins green fluorescent

! Peptide bonds connect the acid end of one amino acid with the amino end of another. ! They are the links that form a protein chain, which can be simple or very complex.

! A Tri-peptide consists of three amino acids linked together. ! When there are three or more amino acids, the protein starts to form three dimensional shapes

POLYPEPTIDE

! Amino acid sequences can vary resulting in almost an endless number of combinations. ! Each proteins sequence is determined by the DNA ! As each amino acid has unique chemical characteristics and electrical charges, the resulting shapes can be very complex. !

! Have compact, spherical shapes. ! Carry out synthesis, transport, and metabolism in the cells. ! Such as myoglobin store and transport oxygen in muscle.

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! Alpha keratins make up hair, wool, skin, and nails. ! Such as feathers contain beta keratins with large amounts of beta-pleated sheet structures.

! DNA in the cell nucleus gives mRNA the instructions. ! mRNA goes into the cellular fluid and attaches itself to ribosomes ! transfer RNA carries free amino acids to the mRNA ! Ribosomes move along the mRNA allowing enzymes to bond one amino acid to another until the completed protein is finished and released.