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Dr.Mayur Sayta Biochemistry Biochemistry Dr.Mayur Sayta Contect details Mob.Number- 9714941350 9016941350 SF-1,2 Samarth tower E Near- Waghodiya Chokdi Baroda- 390025 Sayta Medical Coaching Institute www.mayursayta.com M- 9714941350 Page 1 Biochemistry ENDOPLASMIC RETICULUM (ER) It is a network of interconnecting membranes It is continuous from outer nuclear envelope to outer plasma membrane. It is reticular arrangement It is prominent in cells which are actively synthesizing proteins Proteins, glycoproteins and lipoproteins are synthesized in the ER. Detoxification of various drugs is an important function of ER. ER is classified into two varieties. Rough and Smooth ER looks rough due to ribosomes. It is related with protein synthesis. Smooth ER is related with Lipid synthesis. MITOCHONDRIA Mitochondria is spherical, oval or rod-like bodies. Mitochondria have two membranes. Inner membrane and outer membrane. The inner membrane having folds also known as cristae The inner membrane contains the enzymes of electron transport chain The fluid contains the enzymes of citric acid cycle, urea cycle, etc.. Mitochondria are the powerhouse of the cell. In mitochondria different metabolites are oxidized and energy is stored in the form of ATP. Erythrocytes do not contain mitochondria. Cytochrome P-450 system present in mitochondrial inner membrane is involved in Steroid synthesis. Mitochondria also contain specific DNA. Inner membranes proteins are made by own DNA. Other majority of proteins, especially of outer membrane are synthesized from cellular DNA. Sayta Medical Coaching Institute www.mayursayta.com M- 9714941350 Page 2 Biochemistry PLASMA MEMBRANE The plasma membrane separates the cell from the external environment. It is semi permeable. So entry and exit of compounds are regulated. The membrane is metabolically very active. Structure The structure of the membrane was described as a fluid mosaic model by Singer and Nicolson. Membranes are mainly made up of lipids, proteins and small amount of carbohydrates. The contents of these compounds vary according to the nature of the membrane. Membrane Carbohydrates Carbohydrates are present as glycoproteins and glycolipids. Membrane Lipid Phospholipids are the most common lipids. The phospholipids are arranged in bilayers. Polar head arranged towards outside and hydrophobic parts towards inside. Cell membranes also contain cholesterol. The lipid bilayer shows free movement of its components, so it is also called as fluid in nature. Membrane Proteins The peripheral proteins are situated on the surfaces of the bilayer. The integral membrane proteins are situated inside the bilayer. The integral membrane proteins which are arranged in whole bilayer called transmembrane proteins. The transmembrane proteins can work as receptors. Sayta Medical Coaching Institute www.mayursayta.com M- 9714941350 Page 3 Biochemistry Advertisement me: i have started ug medical coaching class which prepare for mcqs of all exams. student: ug class??? me: yes it is student : but we are going to college for 9 to 5 and got tired so how i can attend? me : its worth for. i take care of subjects from their base and connect it with clinical aspect. i start teaching from students level and take it at some different level i make process of learning enjoyable and easy. A topic that may take hours to understand i clear it in few minutes. student: but fees must be so high?? me: no, its not its vary resnable and i dont ask for fees in one package student: but i hv not herd about any1 going to this type classes how can i? me: if u think medical knowledge should be linked with patients treatment than its going to be vary useful. because u learn base in 1 st and 2 nd year and in 3 rd yr forget every thing so if u have done coaching class than concepts are going to be remembered for long time and will be easy to pass mbbs and will give more confidance in patient's manegement. student: ohk..i will think about it me: ya you should. there is no need to do hurry up in taking decision. just come and sit in free lecture series and than decide. student:--ya thats good idea. so join free lecture series and get some idea...of confident future. For more information log on to www.mayursayta.com Sayta Medical Coaching Institute www.mayursayta.com M- 9714941350 Page 4 Biochemistry CLASSIFICATION OF AMINO ACIDS 1. Based on Structure 1-A. Aliphatic amino acids a. Mono amino mono carboxylic acids: • Simple amino acids: Glycine, Alanine • Branched chain amino acids: Valine, Leucine, Isoleucine • Hydroxy amino acids: Serine, Threonine • Sulphur containing amino acids: Cysteine, Methionine • Amino acids with amide group: Asparagine, Glutamine b. Mono amino dicarboxylic acids: Aspartic acid, Glutamic acid Di basic mono carboxylic acids: Lysine, Arginine 1-B. Aromatic amino acids: Phenylalanine, Tyrosine 1-C. Heterocyclic amino acids: Tryptophan, Histidine 1-D. Imino acid: Proline 1-E. Derived amino acids: 1-E-i. Derived amino acids found in proteins: After the synthesis of proteins, some of the amino acids are modified, hydroxy proline and hydroxy lysine are important components of collagen. Gamma carboxylation of glutamic acid residues of proteins is important for clotting process. In ribosomal proteins and in histones, amino acids are extensively methylated and acetylated. 1-E-ii. Derived amino acids not seen in proteins (Non-protein amino acids): Some derived amino acids are seen free in cells, e.g. Ornithine , Citrulline, Homocysteine. Sayta Medical Coaching Institute www.mayursayta.com M- 9714941350 Page 5 Biochemistry These are produced during the metabolism of amino acids. Thyroxine may be considered as derived from tyrosine. 1-E-iii. Non-alpha amino acids: Gamma amino butyric acid (GABA) is derived from glutamic acid. Beta alanine, where amino group is in beta position, is a constituent of pantothenic acid (vitamin) and co-enzyme A. 2. CLASSIFICATION BASED ON SIDE CHAIN 2-A. Amino acids having nonpolar side chains: These include Alanine, Valine, Leucine, Isoleucine, Aromatic amino acids Methionine, Proline, Phenylalanine and Tryptophan. These groups are hydrophobic (water repellant) and lipophilic. Therefore, the parts of proteins made up of these amino acids will be hydrophobic in nature. 2-B. Amino acids having uncharged or nonionic polar side chains: Glycine, Serine, Threonine, Cysteine, Tyrosine, Glutamine and Asparagine belong to this group. These amino acids are hydrophilic in nature. (Tyrosine and Cysteine may show hydrophobic character when present in the interior of the protein). 2-C. Amino acids having charged or ionic polar side chains (hydrophilic): C-a. Acidic amino acids: They have a negative charge on the R group: Aspartic acid and Glutamic acid (Tyrosine is mildly acidic). C-b. Basic amino acids: They have a positive charge on the R group: Lysine, Arginine and Histidine 3. CLASSIFICATION BASED ON METABOLISM 3-A. Purely Ketogenic Leucine is purely ketogenic because it is converted to ketone bodies 3-B. Ketogenic and Glucogenic Lysine, Isoleucine, Phenylalanine, Tyrosine and Tryptophan are partially ketogenic and partially glucogenic. How ever in humans lysine is predominantly ketogenic. Sayta Medical Coaching Institute www.mayursayta.com M- 9714941350 Page 6 Biochemistry During metabolism, part of the carbon skeleton of these amino acids will enter the ketogenic pathway and the other part to glucogenic pathway. 3-C. Purely Glucogenic All the remaining 14 amino acids are purely glucogenic as they enter only into the glucogenic pathway 4. CLASSIFICATION BASED ON NUTRITIONAL REQUIREMENTS 4-A. Essential or Indispensable The amino acids may further be classified according to their essentiality for growth. Thus Isoleucine, Leucine, Threonine, Lysine, Methionine, Phenylalanine, Tryptophan, and Valine are essential amino acids. Their carbon skeleton cannot be synthesized by human beings and so preformed amino acids are to be taken in food for normal growth. 4-B. Partially essential or Semi-essential Histidine and arginine are semi-indispensable amino acids. Growing children require them in food. But they are not essential for the adult individual. 4-C. Non-essential or Dispensable The remaining 10 amino acids are non-essential, because their carbon skeleton can be synthesized Sayta Medical Coaching Institute www.mayursayta.com M- 9714941350 Page 7 Biochemistry Que. STRUCTURE OF PROTEINS (Organisation of Proteins) Proteins have different levels of structural organization. 1. Primary structure of protein means the order of amino acids in the polypeptide chain. 2. Secondary structure means the relationship of amino acids, close to each other. 3. Tertiary structure means interrelationship of various regions of a single polypeptide chain. 4. Quaternary structure results when the protein is made up of more than one polypeptide chains joined together. 1. Primary Structure Primary structure of protein means the order of amino acids in the polypeptide chain. Each polypeptide chain has a unique amino acid sequence. That sequence is decided by the genes. The primary structure is maintained by the covalent peptide bonds. The peptide bond is a partial double bond. Numbering of Amino Acids in Proteins In a polypeptide chain, at one end there will be one free amino group. This end is called the amino terminal (N-terminal) and the amino acid is named as the first amino acid. At the other end of chain there is a free carboxyl group. It is known as carboxy terminal (C-terminal) and the amino acid is named as the last amino acid. Other amino and carboxyl groups are involved in peptide bond formation. Primary Structure Determines Biological Activity of protein Higher levels of structural organization are dependent on the primary structure. Even a single amino acid change can affect the function of protein. For example, in HbA (normal hemoglobin) the 6th amino acid in the beta chain is glutamic acid; it is changed to valine in HbS (sickle cell anemia). Sayta Medical Coaching Institute www.mayursayta.com M- 9714941350 Page 8 Biochemistry 2. Secondary Structure of Proteins Secondary structure means the relationship of amino acids, close to each other.
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