Professor Teixeira I. What are the structures involved in protein function from

Question

Professor Teixeira I. What are the structures involved in protein function from lower to higher forms? 2, What are all the forces in order from higher to lower strength in the formation and maintenance of the structures involved in protein structure. 3. What is the valence of the carbon atom; what are the groups that bind to the central (alpha) carbon of amino acids? 4. What are the most important chemical bonds between atoms in order of their relative strength? 5. What are the most important chemical bonds between molecules in order of their relative strengths? 6. What are the biologicaly important types of lipids? 7. What are the monomers of carbohydrates and how are they linked? 8. Describe and draw the phospholipid structure and describe the essential cellular structure that it is part of 9. What is the primary structure of a protein, what is another name for it, how is it arranged and why is it in this form? 10. What are the monomeric units of proteins are called and what do we call the bonds that link them. 11. What type of molecules are phospholipids, what type of molecules are lipids 12. What are amino acids, draw a representation of an amino acid, how many amino acids are found in nature, how do they differ from each other and what about those amino acids that do not dissolve in water, where are they found? 13. What is the orbital filling arrangement of un-excited carbon atoms? 12. Draw a 3D representation of a saturated carbon bond, what hybridization state is carbor in these bonds and a 3D representation of a carbon carbon double bond and label the parts of the structures what hybridization state is carbon in these bonds? 13. How does the bond conformation in saturated hydrocarbon chains translate to the overall structure of the hydrocarbon? 14. How does the bond conformation in un-saturated hydrocarbon chains translate to the overall structure of the hydrocarbon? 15. A student forgot to label a beaker containing a DNA solution and a beaker containing a glucose solution. If chemical analysis was performed to identify the contents of each beaker, which of the following would be found in the beaker of DNA but not in the beaker with glucose? A. nitrogen and phosphorus 16, what is an alpha () helix, and where will it be found? 17. What type of bonds are formed by dehydration synthesis between adjacent amino acids? 18. What are the building blocks of an enzyme ? 19. W hat is the lipid group that serves as an energy storage ? 20. What is good biochemistry definition of a saturated fat? 21. List the polysaccharides we discussed? 22. What are the functional groups of amino acids, fatty acids, alcohols, 23. Compare the acidity of a solution of pH 7 and a solution of pH 3.

Explanation / Answer

ANS-1

Proteins are complex molecules. Biochemists have distinguished several levels of the structural organization of proteins. Primary structure, the amino acid sequence, is specified by genetic information. As the polypeptide (a single linear chain of amino acids, held together by amide bonds) chain folds, it forms certain localized arrangements of adjacent amino acids that constitute secondary structure. . The most commonly observed types of secondary structure are the -helix and the -pleated sheet. Both - helix and -pleated sheet patterns are stabilized by hydrogen bonding between the carbonyl and N—H groups in the polypeptide’s backbone. Many fibrous proteins are composed almost entirely of secondary structural patterns.three-dimensional shape polypeptide called tertiary structure.The term tertiary structure refers to the unique three-dimensional conformations that globular proteins assume as they fold into their native (biologically active) structures and prosthetic groups, Proteins that consist of two or more polypeptide chains are called quaternary structure. The oxygen-binding proteins myoglobin and hemoglobin are example of quaternary.

ANS-2

Primary structure it stablize by peptide bond betwen N-H and C=O. Secondery structure is stabilized by hydrogen bonds between N-H and C=O groups.Tertiary structure is stablizing by hydrophobic bonds and quaternary structure is stablized by hydrogen bond.

ANS-3

Valence of carban atom is 4 because the electronic configuration of carban is 1s2 2s2,2p2 .In outer orbital of carban 4 electron are present and it needs 4 other electron to complet the octat(stability).

In amino acid Alpha Carbon contains amine (-NH2), carboxyl (-COOH) functional groups, Hydrogen atom and a side chain (R Alkylic group).

ANS-4

Strong bonds or primary bond such as metallic, covalent or ionic bonds are in the sequence of gigher to lower strength.

Weak bonds or Secondary bond such as dipole–dipole interactions, the London dispersion force and hydrogen are bonding in the sequence of gigher to lower strength.

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