1) Mark the albumins, globulins, prolamins and glutenins on the following state
ID: 198585 • Letter: 1
Question
1) Mark the albumins, globulins, prolamins and glutenins on the following state diagram and determine their molecular weight. kDa 97.2 66.4 44.3 29.0 20.1 14.3 Glutenins (about 50kDa) Prolamins (Any number between 20.1 and 29. kDa) Globulins (Between 14.3 and 20.1 kDa) Albumins (about 12 kDa or below 14 kDa) 2) Give an example of a bitter-tasting chemical compound. a sigroling cascode that prduce ) Define the following terms, the Sci.Sadion o e birerne3S . (a) Protein hydrolysis (b) Peptide bond (c) Protein denaturation (d) Functional foods (e) Protein primary structure Which is amino acid necessary for the quaternary structure of proteins? 4) 5) Describe the primary, secondary, tertiary and quaternary structures of proteins. Draw each structure and explain which chemical bonds participate in each of the protein structures. 6) Draw a -Helix structure and explain what type of chemical bonds we have 7) Explain and draw the -Pleated sheet structure and account for the type ofchemical bonds that participate to stabilize the structure. 8) Chemically define protein denaturation 9) Classify proteins based on the Osborne classification. 10) What is glutenExplanation / Answer
3. a. Protein hydrlolysis is the breaking of protein into its invidual amino acid chains by the enzymes proteases.
b. Peptide bond is the bond formed betwwen to adjacent aminoacid by the condensation reaction between the amino group of one and carboxylic group of other amino acid.
c. Protein denaturation is the process of unfolding of a protein into its primary structure from tertiary or quternary structure by the temperature or pH like factors.
d. Functional foods are the modified foods which provides the nutrients more efficiently than the simple foods.
e. Primary structure of proteins refer to sequence of amino acids in a polypeptide chain along with peptide bonds joining them.
4. Mainly cysteine residues are required to stabilized the quaternary structure by making strong disulfide bonds.
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