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Lara, RMT, MSMT PROTEIN Derived from a Greek word that means of first importance CELLULAR FUNCTIONS OF PROTEINS: a. Enzymes Are biological catalysts Speed up chemical reaction Examples: amylase, pepsin, trypsin, lipase b. Antibodies Also called immunoglobulins Are specific protein molecules produced by specialized cells of the immune system (plasma cells) in response to foreign bodies (antigens) c. Transport Proteins Carry materials from one place to another in the body Examples: transferrin, hemoglobin, myoglobin d. Regulatory Proteins Control many aspects of cell function, including metabolism and reproduction Examples: protein hormones e. Structural Proteins Provide mechanical support to large animals and provide them with their outer coverings Examples: keratin f. Movement Proteins Are necessary for all forms of movements Examples: myosin and actin g. Nutrient Proteins Serve as sources of amino acids for embryos or infants Examples: albumin (egg), casein (milk)

-AMINO ACIDS Building blocks of proteins Amine group (NH2) is attached to the C atom next to the carboxyl group GROUPS OF AMINO ACIDS According to the polarity of their side chains: HYDROPHOBIC AMINO ACIDS Prefer contact with one another over contact with water Generally found buried in the interior of proteins, where they can associate with one another and remain isolated from water 9 amino acids Alanine Valine Leucine Isoleucine Tryptophan

Proline Glycine Methionine Phenylalanine

HYDROPHILIC AMINO ACIDS Attracted to polar water molecules Are often found on the surfaces of proteins 3 Classes 1. Polar, Neutral Amino Acids Have R groups that have a high affinity for water but that are not ionic at pH 7

2. Negatively Charged Amino Acids Have ionized carboxyl groups in their side chains At pH 7 these amino acids have a net charge of -1 They are acidic amino acids because ionization of the carboxylic acid releases a proton

3. Positively Charged Amino Acids At pH 7, have a net positive charge because of their side chains contain positive groups Are basic because the side chain reacts with water, picking up a proton and releasing a hydroxide anion

THE PEPTIDE BOND Amide group that links amino acids Dipeptide the molecule formed by condensing two amino acids N-terminal amino acid with a free N+H3 C-terminal amino acid with a free COO- group NOMENCLATURE PEPTIDES are named as derivatives of the C-terminal amino acid, which receives it entire name For all other amino acids, the ending ine is changed to -yl PRIMARY STRUCTURE OF PROTEINS Is the amino acid sequence of the protein chain It results from the covalent bonding between the amino acids in the chain (peptide bonds) Are translations of information contained in genes SECONDARY STRUCTURE OF PROTEINS Where the peptide chains are folded regularly Is the result of hydrogen bonding between the amide hydrogens and carbonyl oxygens of the peptide bonds TERTIARY STRUCTURE OF PROTEINS Three-dimensional structure Polypeptide chain with its regions of secondary structure further folds on itself QUATENARY STRUCTURE OF PROTEINS Hemoglobin With four individual globular peptide subunits 2 identical alpha-subunits 2 identical beta-subunits CLASSES OF PROTEINS Fibrous Proteins Are tough, insoluble, and composed of fibers and sheets Examples: collagen, keratin, elastins, myosins, fibrin Globular Proteins Are water-soluble and have chains folded into compact shapes Examples: hemoglobin, myoglobin, insulin, immunoglobulins

Simple Protein A protein composed of only of amino acid residues Example: ribonuclease (124 amino acids), albumin Conjugated Protein A protein that incorporates one or more non-amino acid units in its structures Examples: glycoproteins, lipoproteins, metalloproteins DIETARY PROTEINS Nutritional Classes of Amino Acids Essential Amino Acids Are those that cannot be synthesized by the body and are required in the diet Nonessential Amino Acids Are those amino acids that can be synthesized by the body and need not be included in the diet Complete Protein Protein derived from animals It provides all of the essential and nonessential amino acids Incomplete Protein Derived from vegetable sources It lacks a sufficient amount of one or more essential amino acids PHYSICAL AND CHEMICAL PROPERTIES OF PROTEINS Generally tasteless Mostly are colorless, few are colored and crystalline Insoluble in fat solvents and present varied degrees of solubility in water, salt solution, dilute acids, and alkalis Mostly are with high molecular weight Most of them form non-diffusible colloid solutions of the emulsoid type Are amphoteric Most of them are labile and readily modified in solution when subjected to alterations in pH, UV, heat, and organic solvents Very reactive and highly specific PHYSICAL AND CHEMICAL PROPERTIES OF PROTEINS Amphoterism Can act as an acid or base (depends on the pH of the medium) In acid solution its acts like a base In alkaline solution it acts like an acid Principle of electrophoresis If the acidity or alkalinity of the solution is made lass and less, a point will be reached when the amino acid group tends to migrate equally on both directions this pH is called the ISOELECTRIC POINT

Zwitterions or Dipolar Forms Amino acid are completely ionized (zwitterion or dipolar view) but the positive and negative charges neutralizes each other DENATURATION OF PROTEINS Occurs when the organized structures of a globular protein become completely disorganized Temperature As the temperature increases, increases the rate of molecular movement within the solution and the bonds within the proteins begin to vibrate more violently Lose their characteristic 3-dimensional conformation and become completely disorganized 56-60 degrees Celsius Coagulation occur as the protein molecules then unfold and become entangled; they have aggregated to become a solid

pH When the pH of a protein solution is above the pI, all the protein molecules will have a net negative surface charge Below the pI, they will have a net positive charge In either case, these like-charged molecules repel one another, and this repulsion helps keep these very large molecules in solution At the pI the protein molecules no longer have a net surface charge, as a result they no longer strongly repel one another and are at their least soluble Organic Solvents Polar organic solvents denature proteins by disrupting hydrogen bonds within the protein, in addition to forming hydrogen bonds the solvent, water Detergents Have both a hydrophobic region and a polar or hydrophilic region When interacts with proteins, they disrupt the hydrophobic interactions, causing the protein chain to unfold Heavy Metals Mercury or Lead May form bonds with negatively charged side chain groups This interferes with the salt bridges formed between amino acid R group, resulting in loss of conformation

Mechanical Stress Stirring, whipping, or shaking can disrupt the weak interactions that maintain protein conformation HEMOGLOBIN MOLECULE Is a tetramer composed of four polypeptide subunits: 2 alpha-subunits 2 beta-subunits Heme group iron portion Can bind four molecules of oxygen IMMUNOGLOBULINS Antibodies Produced by plasma cells Highly specific Has a memory Can recognize self from nonself Contain 4 peptide chains that are connected by disulfide bonds and arranged in a Yshaped quaternary structure