H HOH ere fem: ao n—G-CL ee at aucss ae eee OH HR OH Oey R Pe hI Tea N-C—C-N-C—C_ +H,0 eet. | he ou R H Protein conformation A prot ¢ or more polypeptide ch: are twisted, and folded upon themselves to form tnacromotecule. This macromolecule has definite three dimensional formation. The function of protein depends upon Form example enzyme can perform its function by This mechanism is possible only due to Many proteins are globular. in consists of on ains. These chains wound shapes called con its conformation. key and lock mechanism. conformation of protein of an enzyme. Some are fibrous Fig: Three levels of protein structures (a) Primary structure (b) Beta pleated sheet, (c) Alpha helix, (d) Tertiary structure, (e) Quaternary structure —“* Mester Success Text Book Of Botany C xin © Levels of Protein Structures per at! al : ; a Each type of protein contains a specitie 1 particule acids. These amino acids are arranged 1% “riyey protein molecule may be coiled and "ie Cera tube brbtetn Se ea form a Unidlhave difler ure, Different kinds of protein ? i Their shapes are related to their pargicat! é A protein molecule has several differen eye rd 1; Primary structure /D! risa The linear sequence of amino acids called imaty structure. For exapi some bs enzyme. It is present in tears, saliva an one 2 Lysozyme is a small proteitf#4t is only cone ee “on The primary structure is like order of letters a x sequence of amino acids in protein is spect tc primary structure can ct protein con! , e, only one F a In this cases 9 function. Its example isSickle 2 e ble to perform its amino acid is not inits proper position. It is unat Trine by function. normally First. primary structure was dete Erederick Sea determined the sequence of insulin hormene- 2. Secondary structure : 3 % The structure formed by folding or coiling of polypeptide chain with the help of hydrogen bonding is called secondary structure. The secondary structure of a protein-is formed by a repeating pattern of bonds (hydrogen bonds) between amino acids. The hydrogen atom attached to nitrogen develops weak electronegative charge. This hydrogen develops affinity for nearby peptidé bond. Thus a weak hydrogen bond is formed. Many such bonds are repeated over long region of polypeptide chain. Such bonds can support particular secondary structures. These structures are: (a) @ helix: A delicate coil of polypeptide chain h os hydrogen bonding between every fourth best by called alpha helix. It was first described by ee 7 bond Robert Corey in 1951. Alpha helix is force eating and lysozyme and a keratin. Tmed in enzyme (b) Pleated sheet: A sheet of poly peptid, fi x folding back and forth of the ee ae formed by the pleated sheet. In this case, two cei th tain is to each other. Hydrogen bonds between the wt 3 lie paraleo a o ire) = a St = StPPP AO SL) mE?)Structure and functions of Biomolecules filamentous protein molecules that form one of the two main classes. of tertiary structife protein, Fibrous proteins are only found in animals. found as an sequences secondary structures, ¢ ous proteins form rod or wire like shapes: ‘These are usually structural or storage proteins. They are water-insoluble. These are fate due to hydraphobie R-groups. The amino acid re not repeated in them. These can form unusual collagen triple helix. The structures often contain cross-links between chains, for example disulfide bonds between keratin chains. Fibrous proteins are used to construct connective tissues, tendons. bone matrix and muscle fiber. Examples of fibrous proteins include keratins, collagens and elastins. (a) (b) Myoglobin, a globular protein Collagen, a fibrous protein Functions of protein Proteins have following physiological functions: ae Proteins as structural material: Proteins are structural material for the animals and plants. Proteins form the major part of the dry weight of animals and plants. Proteins are major part of the all the membranous system of cell. Energy source: Although proteins does not acts as fuel for body but still proteins provide energy to body Protein is broken down into amino acids during digestion. Then deamination of these amino acids takes place. Ammonia is released and ditt rent compounds are’formed, These compounds enter into respiratory pathways (Glycolysis and ‘Krebs cycle) at differen SAYS)2022.05.19 11:28