PROTEIN: types and related disorder.pptx

this presentation will explain each and every points about proteins as well as amino acid. viz-sources. classes ,structure and their related disorder.

1. Proteins Prepared By: Dr Sapna Smith Lal Assistant Professor-Biochemistry Sam Higginbottom University of Agriculture Technology and sciences- Prayagraj

2. Sources

3. What is Protein?

4. Amino Acids are the building blocks of protein- An Amino Acid Dipeptide

5. Peptide Bond/Linkage Peptide bonds are  amide bonds between the α-carboxyl group of one amino acid and the α-amino group of another  with the loss of a water molecule.

6. Group test for identification of proteins A Biuret test is a chemical test used to determine the presence of a peptide bond in a substance. In presence of an alkaline solution, blue-colored copper II ion can form a complex with the peptide bonds The colored coordination complex is formed between Cu2+ ion and carbonyl oxygen (>C=O) and amide nitrogen (=NH) of the peptide bond the solution turns from to purple colour . Biurate Test

7. Classes of Proteins On the Basis of Shape and Size On the bases of Solubility On the bases of Function

8. On the Basis of Shape and Size

9. On the bases of Solubility

10. On the bases of Function

11. Structure of Protein

12. Amino acids  are  organic compounds  that contain  amino  (−NH+3) and  carboxylate  −CO−2  functional groups , along with a  side chain  (R group) specific to each amino acid.  The  elements  present in every amino acid are  carbon  (C),  hydrogen  (H),  oxygen  (O), and  nitrogen  (N) Amino acids are a set of 20 different molecules used to build proteins. Proteins consist of one or more chains of amino acids called polypeptides The amino acid sequences of proteins are encoded in the genes.

13. Types of Amino acid(On Nutritional Bases)

14. Amino Acids Amino acids  are molecules that combine to form proteins . Amino acids and proteins are the building blocks of life.

15. Classification of 20 Amino acids

16. Types of Amino Acids (on the basis of functional group) The acidic amino acids contain  one amino  and two carboxyl groups each, e.g. glutamic acid and aspartic acid. The basic amino acids have two amino groups and one carboyxl group, e.g. lysine and arginine . The neutral amino acids have one amino group and one carboxyl group e.g. alanine , glycine , valine and phenylalanine.

17. Acidic Amino Acid

18. Basic Amino Acid

19. Neutral Amino acid

20. Digestion & Absorption of Proteins

21. Protein Absorption In adults, essentially all protein is absorbed as tripeptides , dipeptides or amino acids and this process occurs in the duodenum or proximal jejunum of the small intestine. The peptides and/or amino acids pass through the interstitial brush border by facilitative diffusion or active transport. In Active transport, sodium and ATP are actively transport the molecule through the cell membrane. The R group determines the type of transporter used. Once passed through the membrane, the amino acids or peptides are released into the intestinal blood stream and are transported to the liver by the hepatic (liver) portal vein. This is known as the enterohepatic circulation. In the liver,they are used to synthesize protein, nitrogen containing compounds and form purine / pyrimidine bases. In some cases, they may be converted to energy. The liver regulates the amino acid levels in the blood. The amino acids that do not stay in the liver, pass through and are transported to the rest of the body to be taken up and utilized by other cells.

22. Protein Metabolism various  biochemical  processes responsible for the synthesis of  proteins  and  amino acids  (anabolism), and the breakdown of proteins by  catabolism . The steps of protein synthesis include transcription, translation, and post translational modifications. Proteins are first broken down to individual amino acids by various enzymes and  hydrochloric acid  present in the gastrointestinal tract. These amino acids are absorbed into the bloodstream to be transported to the liver and onward to the rest of the body. Absorbed amino acids are typically used to create functional proteins, but may also be used to create energy. They can also be converted into glucose. This glucose can then be converted to triglycerides and stored in fat cells. Proteins can be broken down by enzymes known as peptidases or can break down as a result of  denaturation . Anabolism Catabolism

23. Biological active compounds derived from amino acid and proteins The amino acids are an important group of compounds concerned in the biosynthesis of a variety of nitrogen-containing plant metabolites, including  proteins, enzymes, nucleic acids, hormones, chlorophyll, amines, alkaloids, cyanogenic glycosides and glucosinolates . In humans, Amino acids are not only protein precursors, but also precursors for numerous other crucial compounds, such as  polyamines, S- adenosylmethionine , pantothenic acid, and nucleotides .

24. Cont….. The hormones derived from amino acids include  catecholamines , serotonin, melatonin, and the thyroid hormones thyroxine and triiodothyronine . The basic structural unit of an antibody molecule consists of four polypeptide chains,  two identical light (L) chains (each containing about 220 amino acids) and two identical heavy (H) chains (each usually containing about 440 amino acids) .

25. PROTEIN DISORDERS

26. PROTEIN UREA Proteinuria is a broad term used to describe protein in the urine. It is a general term for the presence of proteins, including albumin, globulin, Bence -Jones protein, and mucoprotein in the urine. In healthy persons, urine contains  very little protein an excess is suggestive of illness. Excess protein in the urine often causes the urine to become foamy (although this symptom may also be caused by other conditions). Severe proteinuria can cause  nephrotic syndrome  in which there is worsening swelling of the body.

27. HYPOPROTEINEMIA Hypoproteinemia is  a condition in which a person has very low protein levels in the blood . Common symptoms include fatigue, weakness, and susceptibility to infection.  Hypoproteinaemia can be caused by malnutrition or malabsorption due to intestinal disease, by excessive loss of plasma protein either into urine ( nephrotic syndrome) or into the gut lumen (protein-losing enteropathy ), or by hepatic failure, Decreased serum protein reduces the oncotic pressure of the blood, leading to loss of fluid from the intravascular compartment, or the blood vessels, to the interstitial tissues, resulting in edema. This is termed as hypoproteinemia .

28. Hypergammaglobulinemia refers to the  overproduction of more than one class of immunoglobulins by plasma cells . It is most commonly associated with liver disease, acute or chronic inflammation, autoimmune disorders, and some malignancies. Chronic infections such as malaria,  endocarditis ,  trypanosomiasis , HIV, and infections associated with  cystic fibrosis  increase circulating immunoglobulin levels well above the normal range. 

29. ELECTROPHORESIS Principal and pattern

30. Principal Serum protein electrophoresis is an electrophoretic method of separating proteins present in the serum to various fractions based on their molecular weight and electric charges. Electrophoresis had been widely used in clinical medicine for aiding in diagnosis of various clinical conditions like acute and chronic inflammations, monoclonal gammopathies , nephropathy, liver diseases, etc. Proteins are ampholytes that can acquire a positive or negative charge depending on the pH of the buffer in which the electrophoresis takes place . If a mixture of charged particles is exposed to an electric field, the molecules of the substances begin to move.

31. PATTERN The electrophoretic patterns of a series of normal and pathological human sera and plasmas  have been obtained using the schlieren scanning method. From these patterns the mobilities and concentrations of the electrophoretically distinct protein components have been computed.

32. In born error of amino acid metabolism

33. Inborn errors of amino acid metabolism are  metabolic disorders which impair the synthesis and degradation of amino acids . Inborn errors of amino acid metabolism result from a mutation in the gene responsible for making the enzyme involved in the amino acid synthesis pathway. There are around 50 errors known so far, but generally their incidence is very rare. Phenylketonuria is the most common one. Most of these errors are routinely tested right after birth.

34. Inborn Diseases of Amino Acid Metabolism Phenylketonuria (Most common) Maple Syrup Urine Disease Albinism Homocystinuria Alkaptonuria

35. PHENYLKETONURIA: Most Common disease of amino acid metabolism Due to deficiency of Phenylalanine hydroxylase enzyme (PAH) Phenylketonuria , also called PKU, is a rare inherited disorder that causes an amino acid called phenylalanine to build up in the body. PKU is caused by a change in the phenylalanine hydroxylase (PAH) gene. This gene helps create the enzyme needed to break down phenylalanine.

36. The signs and symptoms of PKU vary from mild to severe. The most severe form of this disorder is known as classic PKU. Infants with classic PKU appear normal until they are a few months old. Without treatment, these children develop permanent intellectual disability. Seizures, delayed development, behavioral problems, and psychiatric disorders are also common. Untreated individuals may have a musty or mouse-like odor as a side effect of excess phenylalanine in the body. Children with classic PKU tend to have lighter skin and hair than unaffected family members and are also likely to have skin disorders such as eczema. Less severe forms of this condition, sometimes called variant PKU and non-PKU hyperphenylalaninemia , have a smaller risk of brain damage.

37. ALBINISM

38. Plasma Protein: Types, Function and Normal Value

39. Plasma proteins are proteins present in the blood plasma and are produced by the liver (except for immunoglobulins ) The proteins are produced by the rough ER in hepatocytes and exported into the blood via the Golgi complex There are a number of different types of plasma proteins, each serving different specific functions: Albumins regulate the osmotic pressure of the blood (and hence moderate the osmotic pressure of body fluids) Globulins participate in the immune system (i.e. immunoglobulins ) and also act as transport proteins Fibrinogens are involved in the clotting process (soluble fibrinogen can form an insoluble fibrin clot) Low levels of other plasma proteins have various functions (e.g. α-1-antitrypsin neutralises digestive  trypsin )

40. Normal value of Plasma protein