BLG 143 Study Guide - Final Guide: Covalent Bond, Ionic Bonding, Hydrophile

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redrhinoceros565

25 Apr 2018

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3. 3 proteins are the most versatile large molecules in cells. Proteins are crucial to most tasks required for cells to exist: catalysis, many proteins are specialized to catalyze or speed up chemical reactions. A protein that functions as a catalyst is called an enzyme: defence, movement, signalling, structure (mechanical support, transport (move substances through body haemoglobin) Proteins can serve diverse functions in cells because they are diverse in size and shape as well as in the chemical properties of their amino acids. No matter how large or complex a protein may be, its underlying structure can be broken down into 4 basic levels of organization. The unique sequence of amino acids in a protein single amino acid change can radically alter protein function. of protein structure. Because the amino acid r-groups affect a polypeptide"s properties and function, just a. A protein"s primary structure is fundamental to its function, as well as to the higher levels.

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magentahare115

Please help! Not sure about these questions..thanks

QUESTION 1

An example of an endergonic reaction is

	A.	Polymerizing a protein from amino acids.
	B.	Breaking a protein down into amino acids.
	C.	Breaking down ATP into ADP and P.
	D.	Breaking down glucose (using oxygen) to make CO2 and H2O.

QUESTION 2

When ATP breaks down to supply energy for cellular reactions, it often transfers its 3rd phosphate to another molecule. This is called ______, and makes the other molecule _______ reactive.

	A.	catalysis . . . more
	B.	phosphorylation . . . more
	C.	phosphorylation . . . less
	D.	polymerization . . . less

QUESTION 3

Which is true of enzymes?

	A.	They are highly specific in the reactions they catalyze.
	B.	Chemically, most are carbohydrates.
	C.	They accelerate reactions by adding energy.
	D.	They break down and are used up as they catalyze reactions.

QUESTION 4

What is peristalsis?

	A.	Rings of muscle that can contract to close off the stomach at each end.
	B.	A gland that secretes saliva.
	C.	Coordinated muscle contractions that move the contents of the GI tract.
	D.	A stomach enzyme that breaks down proteins.

QUESTION 5

Which is not a component of gastric juice?

	A.	H2O
	B.	acid
	C.	pepsin
	D.	amylase

QUESTION 6

What does the enzyme pepsin do?

	A.	Completely breaks down proteins into individual amino acids.
	B.	Completely breaks down carbohydrates into monosaccharides.
	C.	Partially breaks down proteins into smaller polypeptides.
	D.	Partially breaks down fats into fatty acids.

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.

BLG 143 Study Guide - Final Guide: Covalent Bond, Ionic Bonding, Hydrophile

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