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HTT106 Health And Safety In Travel And Tourism

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HTT106 Health And Safety In Travel And Tourism Question: Use publisher to produce a trifold brochure with 3 columns on A4 size (3 columns each size as double sided, so 6 all together) -Provide a photo and description of the primary, secondary, tertiary and quaternary levels of structure. -Give an explanation of the roles of hydrogen, ionic and covalent bonding in maintaining the protein structure. -Give an overview of the proteins biological role, and the ways in which its structure allows it to perform its role. -Label the diagrams secondary structure where there is a helix and/or b pleated sheet present AND discuss if the b pleated sheet is anti parallel or parallel. Answer: Amylase is an enzyme that plays an important role in the hydrolysis of starch and converts it to sugar. Amylase is primarily present in the saliva of mammals, including humans (Imam et al. 2013). Foods containing large quantities of starch such as, potatoes and rice often acquire a sweet taste while chewing due to the action of amylase that degrades starch into sugar. All amylases are referred to as glycoside hydrolase and exert their action on α-1,4-glycosidic bonds. · The primary structure of amylase comprises of amylose that is a straight-chain α-1,4 linked polymer. · This polymer is made up of an estimated 105units and amylopectin, which is a branched chain polymer having α1,4 linked glucose. · The branch points are made up of α-1,6 linkages that comprise of 106 glucose units. The secondary structure of amylaseis 26% helical. Amylase comprises of 20 alpha helices that are made up of 133 residues. Amylase also has 23% beta sheet. The quaternary structure of amylase comprises of five disulfide bridges that facilitate the structure formation These bonds are formed between residues 28-86, 70-115, 141-160, 378-384, and 450-462. The image given below represents the bond between 28-86, and 384-78. · Hydrogen bonds are formed in between Asp300 and Trp58. · Gly306 and Ala307 play an important role in providing a hydrophobic surface to protect the substrates. · Van der Waals interactions present between two or more atoms is the weakest form of intermolecular attraction. · Amylase contains two active residues located at position 193 and 233. · The residue 193 acts in the form of a nucleophile · The residue 233 acts in the form of a proton donor. Three subunits namely, subunit A, B and C are present. Prediction of protein subcellular localization comprises of predicting the location where a protein is present, commonly referred to as, subcellular localization. There are a range of databases that are used for subcellular localization prediction such as, the lactic acid bacterial secretome database, UniProtKB, and Compartments. Change in pH and ion concentration alters electrostatic interaction. Proteins are found to change their shape in response to the surrounding environment. The common changes that affect their structure are pH, solvent polarity, temperature, and concentration of ions sticking to the protein. Temperature changes reduce hydrogen bond length Reducing agents break disulfide bonds between cysteine residues. References Binder, J.X., Pletscher-Frankild, S., Tsafou, K., Stolte, C., O’Donoghue, S.I., Schneider, R. and Jensen, L.J., 2014. COMPARTMENTS: unification and visualization of protein subcellular localization evidence. Database, 2014. Imam, H., Mahbub, N.U., Khan, M.F., Hana, H.K. and Sarker, M.M.R., 2013. Alpha Amylase Enzyme Inhibitory and Anti-in?ammatory Effect of Lawsonia inermis. Pakistan Journal of Biological Sciences, 16(23), pp.1796-1800. National center for biotechnology information, (2018). PDB ID 1SMD: Human Salivary Amylase. Available from https://www.ncbi.nlm.nih.gov/Structure/icn3d/full.html?&mmdbid=57381&bu=1&showanno=1 Accessed on 30 November 2018. Uniprotkb, (2018). P04745 (AMY1_HUMAN). Available from https://www.uniprot.org/uniprot/P04745 Accessed on 30 November 2018.

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