BSC-2010 Chapter Notes - Chapter 5: Sucrose, Glycosidic Bond, Dehydration Reaction

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greyskunk797

25 Apr 2017

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What component of amino acid structure varies among different amino acids? the components of the r-group. The carboxyl group (cooh) contains two oxygen atoms that tend to pull electrons away from the hydrogen atom, so this group tends to lose a proton and is acidic. When a protein has been unfolded enough to lose its function, the protein has been what? denatured. The helical foldings in proteins what? are kept folded by hydrogen bonds. It can form both polar and nonpolar bonds. The majority of their bonds are nonpolar covalent carbon-to-hydrogen linkages. They have variations in arrangement around a double bond. Which of the functional groups below acts most like an acid in water? carboxyl. A hydrocarbon skeleton is covalently bonded to an amino group at one end and a carboxyl group at the other end. When placed in water this molecule would function _____. as an acid and a base.

Related Questions

1. The level of protein structure that is stabilized primarilyby non-covalent interactions between the side chains within asingle polypeptide chain is refered to as its:

A) primary structure

B) secondary structure

C) tertiary structure

D) quaternary structure

E) none of the above

2. Collagen, a strong fibrous protein found in connectivetissue, bone, and the extracellular matrix, has a structure inwhich three left-handed helices wind around each other to form aright-handed triple helix. The primary structure of collagen has arepeat unit of -(Gly-X-Pro)- Which of the following bonds stabilizethe collagen triple helix? (mark all that apply)

A) Hydrogen bonds between hydroxyproline residues

B) Hydrogen bonds between N-H and C=O

C) Ionic bonds between amino acid side chains

D) Hydrogen bonds between charged amino acids

3. The non-covalent forces that stabilize the Beta-strandconformation of peptides include:

A) H-bonds between amide C=O and amide NH

B) Van der Waals packing between the peptide backbone atoms

C) Van der Waals packing due to side chain interdigitation

D) Only A and B above

E) None of the above

4. What is the approximate length difference of a 22-kDasingle-stranded ?-helical protein segment vs. a 22-kDasingle-stranded ?-strand protein segment? Assume a mean residuemass of 110 Da. Show work.

5. Circular dichroism measurements have shown that the peptidebackbone of poly-l-lysine (KKKKKKK) adopts a random coilconformation at pH 7.0, but becomes ?-helical as the pH is raisedabove 10. This observation is known as the

magentaotter572

Please check P1&P2 & help with P3

P1.

A. DNA

B. Glycogen

C. Ribosome

D. miRNA

E1. Triacylglycerol

E2. Cyclic AMP

F. Acetyl CoA

G. Testosterone

H. ATP

I. Tau

1. Which molecules contain nucleotides? A, H, F, E2, D, C?

2. Which molecules contain at least one fatty acid? E1

3. Which molecules contain amino acids? I

4. Which molecules contain a sugar? A, B, H, E2, D, F

P2.

A. Phospholipid

B. Glycolipid

C. Cholesterol

D. None

1. Which molecules are amphipathic? A, B, C

2. Which molecules would decrease fluidity of plasma membrane? A?, B?, C

3. Which molecules are important for cell-cell recognition? B?

4. Which molecules are located solely on the intracellular surface of the plasma membrane, facing the cytosol? D

P3. 1. Describe where the following amino acids would be found in the glucose transporter (GLUT2) - part of the protein exposed to the lipid bilayer or within the interior of the transporter - and provide reasoning.

1A. Valine

1B. Serine

Acidic, basic, nonpolar, uncharged polar

2. Which amino acids form hydrogen bonds that shape tertiary structure?

3. Which amino acids allow transmembrane proteins to span the lipid bilayer?

1. What is an organic molecule?

2.Name three hydrocarbons and be able to draw their structural formulas.

3. What is an isomer? List and describe the three types (structural, geometric, and enantiomers).

4. Be able to recognize and describe the properties of these functional groups: aldehyde, ketone, hydroxyl, sulfhydryl, carboxyl, amino, and phosphate groups.

5. What is a monosaccharide? Give two examples of these molecules and their functions.

6. Describe these chemical reactions: dehydration synthesis (condensation reaction) and hydrolysis (rehydration).

7. What is a disaccharide? List two and give their functions.

8. What is a polysaccharide? List two storage forms and two structural forms. How are they formed and what is their specific function?

9. How do the pancreatic hormones insulin and glucagon regulate blood sugar levels?

10. What is molting and why is it necessary in certain animals?

11. What four molecules are bonded together to form a triglyceride or fat? Why are fats nonpolar? What are some functions of fats as well as other lipids such as oils and waxes?

12. How do saturated and unsaturated fats differ? Discuss bonding patterns and possible sources of these fats. Which type is healthier for you? Why?

13. Why do animals store most of their excess glucose as fats or oils rather than as glycogen or protein? Give two reasons.

14. What are phospholipids? Identify parts of the phospholipid bilayer that are hydrophobic or hydrophilic? What important cell structure do these molecules help create?

15. Describe the structure of a steroid. How is cholesterol used in beneficial ways in your body?

16. What are LDLs and HDLs? Which is considered good or bad cholesterol? What condition could result from high blood pressure?

17. What are four ways to either reduce high blood cholesterol or maintain a safe level?

18. What is the composition of an amino acid? Why would they be considered nonpolar, polar, acidic, or basic?

19. Define dipeptides and polypeptides.

20. Describe the primary structure of a protein. What type of bonding creates it?

21. What is the secondary structure of a protein? Name two types of secondary structure and indicate what type of bonding holds them together. List three fibrous proteins.

22. What is the tertiary structure of a protein? What types of bonds or chemical interactions allow a protein to maintain this structure? List three globular proteins.

23. What is the quaternary structure of a protein? Describe a hemoglobin molecule.

24. What are the subunits of nucleic acids and what is their composition? How are these subunits bonded together? What is DNS's basic shape?

25. List three differences between DNA and RNA.

BSC-2010 Chapter Notes - Chapter 5: Sucrose, Glycosidic Bond, Dehydration Reaction

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