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Proteins and Amino Acids

Department of Biochemistry and Molecular Biology Tarumanagara Univ. School of Medicine.

Natural Proteins
“Polymers consisting of widely varying numbers and combinations of about 22 individual amino acids linked by peptide bonds in various alignments and shapes.”

Plants synthesize all 22 AA’s. Animals synthesize only 11-14. Rest (8-11) are “dietary essentials.”

Peptide Bond
“Bonds that couple the alpha carbonyl group of one amino acid residue to the alpha amino group of another residue.”

Peptide bond

Based on shapes and solubilities I. dilute acids or bases or alcohol II. Fibrous Proteins Insoluble in water. resistant to digestive enzymes III.Classification of Proteins . Globular Proteins Soluble in water. Conjugated Proteins Amino acids bound to some type of non-amino group .

Varies by: species. age.Proteins Differ Greatly in “Quality” Quality of a protein is high if it contains all of the essential amino acids in the proper ratios for a specific animal. gender. productive function .

Alpha Amino Acid Acid = = Carboxyl Amino = NH2 General Structure .

__________________ . Albumins.Soluble in water .Some contain carbohydrate (CHO) -Therefore. Globular Proteins A. Egg and Serum .Coagulated by heat . are “conjugated proteins” also.I.

Soluble in salt solutions.Insoluble in water .Heat labile .I. serum globulin (also a glycoprotein) __________________ . Globular Proteins B. Globulins. myosinogen.  80% of oilseed proteins . legumin of peas. NaCl .Examples: fibrinogen. glycinin in soybean.

Soluble in ethanol .Examples: Zein in corn Hordein of barley Gliadins of wheat. barley . .Soluble in dilute acids or bases __________________ Prolamines . wheat.I. Globular Proteins C. Glutelins.Insoluble in water. rye _________________ D. corn. neutral saline .

Histones .Examples: globin. part of hemoglobin __________________ . Globular Proteins E. RNA . DNA.I.“Basic” proteins .Often combined with nucleic acids.Excess of basic amino acids .

Insoluble without treatment . skeletal connective tissue . Fibrous Proteins A.II. Collagens.No cystine.Large amounts of hydroxyproline . cysteine or tryptophan __________________ .Changed into digestible gelatins by boiling .

Fibrous Proteins B.Poorly digested . Elastins.Similar to collagens . tendons and arteries .II.Cannot be converted to gelatin .High in lysine ________________ .

Treatment with heat and pressure  Cystine to 5-6% breaks –S-S. Fibrous Proteins C.Very insoluble & indigestible. zero . Keratins. 14-15% . beaks .High cystine.II.bonds  Digestibility to 70-80% __________________ . claws. hair. feathers.

galactosamine B. i. glucosamine.. . Conjugated Proteins A.Examples ribonucleoprotein deoxyribonucleoproteins Mucoproteins . Nucleoproteins .e.With mucopolysaccharides.III.With nucleic acids .

Lipoproteins .Example: in egg albumin D.< 4% CHO. Glycoproteins .Water soluble proteins with: lecithin cephalin cholesterol other lipids or phospholipids . Conjugated Proteins C. hexose .III.

Examples: hemoglobin cytochromes flavoproteins visual purple of retina .simple protein to a colored prosthetic group .III. Chromoproteins . Conjugated Proteins E.

Protein . Blood Globulins Albumin Globin Fibrinogen Lipoproteins . muscle myofibrilar contractile 2. Organs and soft tissues. Structural proteins Collagen Elastin Keratin 3.Functions 1.

Body Metabolism Enzymes digestive (Table 4. 128 PTH.Protein . rapid to slow (See Table 9.4) Hormones Examples? Page. _______.3) degradative (Table 9. _______ Immune antibodies Hereditary transmission .Functions 4.5) synthesis.

AA. 135-136 in Text) alanine  PA + NH3 Also.Protein . BA. Source of energy after deamination (pp. VA.Functions 5. IVA .

Classification (pp 121-122 in Text) Neutral Aliphatic Aromatic Sulfur-containing Acidic Basic Imino .Amino Acids .

Neutral Amino Acids 1) Aliphatic Glycine Alanine Serine Threonine Valine Leucine Isoleucine Alanine .

Neutral Amino Acids (2) Aromatic amino acids (a) Phenylalanine (b) Tyrosine .

Neutral Amino Acids (2) Aromatic amino acids (c) Tryptophan Indol .

Neutral Amino Acids 3) Sulfur-containing: AA + Thiol(s) Cysteine Alanine + HS Cystine 2 Cysteines with -S-SMethionine .

Neutral Amino Acids (3) Sulfur-containing amino acids (a) Cystine (b) Cysteine .

Neutral Amino Acids (3) Sulfur-containing amino acids (c) Methionine .

Acidic Amino Acids 2 Hydroxyl groups Aspartic Acid 4 C’s Glutamic Acid 5 C’s .

Acidic Amino Acids (1) Aspartic acid (2) Asparagine .

Acid Amino Acids (3) Glutamic acid (4) Glutamine .

Basic Amino Acids 2 NH2’s Arginine Histidine Lysine .

Imino Amino Acids NH2 not on alpha carbon Rings. pyrolidine Carboxylic acids .

Imino Acids (1) Proline 2) Hydroxyproline .

and D-Amino Acids Schematic .L.

up to 50% of methionine requirement D-Threonine. D.have no function. 60% for pig . up to 25%.Amino Acid Isomers Biological Activity Animal Tissues – All 22 are L-isomers. D-Tryptophan. Diet – All must be L-isomers except: D-Methionine.

Threonine. 80-100% relative activity .8% L-Lysine Lysine. Methionine MHA. Tryptophan.Amino Acid Isomers Biological Activity Synthetic AA’s Via recombinant DNA technology Most sold as salts: Lysine HCl = 78.

Varies by: Species Stage of life cycle Productive function Maintenance vs milk .Essential/Nonessential AA’s All 22 are required for protein synthesis/metabolism Dietary essential/Indispensable = Those not synthesized in animal tissues of most species in sufficient amounts to meet metabolic needs without being added to diet. Others are nonessential.

Essential Amino Acids. Rats Rose. 1948 PVT TIM HALL A H I L L M P T T V Arginine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Threonine Tryptophan Valine .

Essential Amino Acids A H I L L M P T T V Arginine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Threonine Tryptophan Valine B B N N B N-S N-R N N-R N .

Essential Amino Acids A H I L L M P T T V T P Arginine – for maintenance Histidine – for maintenance Isoleucine Leucine Lysine Methionine/Cystine Phenylalanine/Tyrosine Threonine Tryptophan Valine Taurine – Cat Proline (-Amino sulfonic) .