Documente Academic
Documente Profesional
Documente Cultură
What is PROTEIN?
It is a naturally occurring, unbranched polymer in which the monomer units are amino acids.
A large complex organic compounds composed of amino acids as the building units linked together in peptide bonds.
CHARACTERISTICS
1. 2.
Presence of nitrogen
15.4% by mass (average nitrogen content of proteins)
Other elements such as phosphorus and iron are essential constituents of certain specialized proteins.
Casein- main protein of milk, contains phosphorus Hemoglobin- oxygen- transporting protein contains iron.
1. 2.
Structural Proteins- confers stiffness and rigidity to otherwise fluid-like biochemical systems. E.g., collagen
Transmembrane Proteins- help control the movement of small molecules and ions through the cell membrane. Storage Proteins- bind and store small molecules for future use, e.g., ferritin, myoglobin
Regulatory Proteins- control the expression of genes, and thereby regulate the kind of proteins manufactured in a particular cell and control when such manufacture takes place.
Nutrient Proteins- important in the early stages of life from embryo to infant. E.g., casein, and ovalbumin
Non polar amino acid- contains one amino group, one carboxyl group and a
non polar side- chain, when incorporated into a protein they are hydrophobic generally found in the interior of proteins. - Glycine , Alanine , Valine , Leucine , Isoleucine , Proline , Phenylalanine , Methionine , & Trytophan
POLAR NEUTRAL AMINO ACID - contains one amino group, one carboxyl group and a side- chain that is polar but neutral. - Serine , Cysteine , Threonine , Asparagine , Glutamine , Tyrosine
CHIRALITY
Four different groups are attached to the - carbon in all of the standard amino acids (except glycine, where the R group is a hydrogen atom)
Amino acids are charged species both in the solid state and in solution
Both an acidic group (-COOH) and a basic group (-NH2 ) are present in the same carbon in an - amino acid.
ZWITTERIONS
Compounds that has a positive charge on one atom and a negative charge on another, but which has no net charge. Comes from the German zwitter, meaning double ion. The net charge on a zwitterion is zero even though parts of the molecule carry charges in solution and also in the solid state - amino acids exists as zwitterions. In an acidic solution, the zwitterion accepts a proton (H+) to form a positively charge ion. In basic solution, NH3 of the zwitterion loses a proton, and a negatively charge species is formed.
ISOELECTRIC POINTS
NAME ISOELECTRIC POINT 6.01 10.76 5.41 2.77 5.07 3.22 5.65 5.97 7.59 6.02 5.98 9.74 5.74 5.48 6.48 5.68 5.87 5.88 5.66 5.97
The pH at which an amino acid solution has no net charge because an equal number of positive and negative charges are present, every amino acid has a different isoelectric points. ELECTROPHORESIS the process of separating charged molecules on the bases of their migration toward charged electrodes associated with an electric field.
Alanine Arginine Asparagine Aspartic acid Cysteine Glutamic acid Glutamine Glycine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Prolein Serine Threonine Trytophan Tyrosine Valine
The only standard amino acid that has a side- chain that contains sulfhydryl group ( -SH group).
Cysteine, in the presence of mild oxidizing agents readily dimerizes, that is, reacts with anothes cysteine molecule to form cystine molecule. ( a dimer is a molecule that is made up of two like subunits) The presence of cysteine has important consequences for the chemical structure and shape of protein molecules it is a part of. The S-S bond is called a disulfide linkage.
PEPTIDE NOMENCLATURE
IUPAC rules for naming small peptides: RULE 1: The C- terminal amino acid residue ( located at the far right of the structure) keeps it full amino acid name. RULE 2: All of the other amino acid residues have names that end in yl . The yl suffix replaces the ine or ic acid ending of the amino acid name , except for trytophan ( trytophyl ), cysteine ( cysteinyl ), glutamine ( glutaminyl ), and asparagine ( asparaginyl ). RULE 3: The amino acid naming sequence begins at the N- terminal amino acid residue.
Solution: glutamic acid becomes glutamyl serine becomes seryl alanine remains alanine Answer:
glutamylserylalanine
Isomeric Peptides
Peptides that contain the same amino acids but in different order are different molecules ( constitutional isomers ) with different properties The number of peptides possible increases rapidly as the length of the peptide chain increases.
Vasopressin regulates the excretion of water by the kidneys, it also affects blood pressure.
Enkephalins- pentapide neurtransmitters produced by the brain itself that bind at receptor sites in the brain to reduce pain.
The two enkephalins differ structurally only in the amino acid at the end of the chain
- A triteptide present in significant concentrations in most cells & is of considerable physiological importance as a regulator of oxidation reduction reactions. - functions as an antioxidant , protecting cellular ccontents from oxidizing agents such as peroxides & superoxides ( highly reactive forms of oxygen often generated within the cell in response to bacterial invasion ) BHA & BHT & - carotene
Monomer Protein Protein in which only one peptide chain is present Multimetric Protein - Protein in which more than one peptide chain is present Protein subunits - is the peptide chain present in in multimetric proteins
Prosthetic group- non-amino acid components that may be organic or inorganic. - non-amino acid group present in a conjugated protein
Class
Hemoproteins
Lipoproteins
Prosthetic Group
Hemi unit Lipid
Specific Example
Hemoglobin Myglobin LDL HDL Gamma globulin Mucin Interferon
Function of example
Carrier of O2 in blood O2 binder in muscles Lipid carrier Lipid carrier Antibody Lubricant in mucous secretions Antiviral protection Enzyme in glycogen phosphorylation Site for protein synthesis Self-replicating infection complex Storage complex for iron Enzyme in alcohol oxidation
Glycoproteins
Carbohydrate
Phosphoproteins Nucleproteins
metalloproteins
Metal Ion
Quaternary Structure
- The organization among the various peptide chains in a multimeric proteins. - The three dimensional shape of a protein consisting of 2 or more independent peptide chains, which results from noncovalent interaction between R groups.
Controls glucose metabolism Involved in Oxygen storage in muscles Involved Oxygen transport in blood Involved iron transport in blood Involved in immune system responses
- keratin
A fibrous protein particularly abundant in nature
Major protein constituent of hair, feathers, wool, fingernails and toenails, claws, scales,horns,turtle shells, quills , & hooves THE COILED COIL STRUCTURE OF THE - keratin.
Collagen
The most abundant of all proteins in humans ( 30 % of total body protein ) Major structural material in tendons, ligaments, blood vessels, and skin. Organic component of bones & teeth
Tissue
Achilles Aorta Bone ( mineral- free ) Cartilage Cornea Ligament Skin
Collagen (% by mass )
86 12-24 88 46-63 68 17 72
Hemoglobin
a globular protein that transports oxygen from the lungs to tissue. Tetramer,has four peptide chains & four heme units
STRUCTURE OF THE HEME GROUP:
Myoglobin
A globular protein that functions as an oxygen storage molecule in muscles. Monomer , consist of a single peptide chain & a heme unit. Has higher affinity for oxygen than does hemoglobin
Protein Hydrolysis
When a protein or smaller peptide in a solution of strong acid or strong base is heated, the peptide bonds of the amino acids are produced. Hydrolysis reaction is the reverse of the formation reaction for a peptide bond. Protein hydrolysis produces free amino acids The process is the reverse of protein synthesis, where free amino acids are combined. Hydrolysis of a protein in acidic solution: H+ H+ Protein + H2O ------------- smaller peptides--------------amino acids
Protein Denaturation
Is the partial or complete disorganization of a proteins characteristics threedimensional shape as a result of disruption of its secondary, tertiary, and quaternary structural interactions. The result of denaturation is loss of biochemical activity,loss of the proteins three-dimensional structure.Complete loss of such structure produces an unsaturated protein stand. It does not affect the primary structure of a protein Loss of water solubility is a frequent physical consequence of protein denaturation. Renaturation- restoration process, in which the protein is refolded Coagulation- the precipitation out of biochemical solution of denatured protein. EXAMPLE of protein denaturation: Egg white is poured onto a hot surface Protein-containing foods are cooked Process of giving a hair permanent
Glycoproteins
Is a Protein that contains carbohydrates or carbohydrate derivatives in addition to amino acids When boiled in water , under basic conditions, it is converted to the water-soluble protein gelatin. Include a number of very important substances: TWO OF THESE: Collagen & Immunoglobins
Collagen
Classified ads glycoprotein because of the presence of of carbohydrate units in its structure.
Immunoglobins
Are among the most important & interesting of the soluble proteins in the human body Is a glycoprotein produced by an organism as a protective response to the invasion of microorganisms or foreign molecules Serves as antibodies to combat invasion of the body by antigens . Antigen- a foreign substance , such as bacterium or virus, that invades the human body. Antibody- a biochemical molecule that counteracts a specific antigen.
Lipoproteins
Is a conjugated protein that contains lipids in addition to amino acids. Major function is to help suspend lipids & transport them through the bloodstream. Insoluble in blood because of their non-polar nature The density is related to the fractions of protein & lipid material present.The greater the amount of protein in the lipoprotein, the higher the density
PLASMA LIPOPROTEIN
- A lipoprotein that is involved in the transport system for lipids in the bloodstream.
Protein regulates osmotic pressure, hence water balance & acid- base balance
Helps in the exchange of nutrients & other metabolites which pass between cells & the intercellular fluids or between tissues & the blood or lymph( extracellular fluids )
MARASMUS
Condition resulting from from severe malnutrition, afflicts very young children who lack both energy & protein foods as well as vitamins & minerals.
Kwashiorkor
Appears when there is a sudden or recent lack of protein containing food. Causes fat to accumulate in the liver