Biology 1002B Lecture Notes - Lecture 3: Sulfide, Heme, Beta Sheet

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erinbutterfly486

26 Apr 2016

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Vary largely due to chemical composition and function. Speed up movement of substances across biological membrane. Promote or inhibit the activity of other cellular molecules. Bind molecules at cell surface or within cell. Hold amino acids and other substances in stored. Chaperone protein: specific type of protein that facilitates new proteins to fold correctly: may be called on when the protein forms or later on if the protein is damaged. Unfolding proteins: denaturing refers to the unfolding of a protein from its active conformation: usually results in loss of function, proteins in nature can change due to ph levels, temperature, can repair in renaturation. Amino acids: contain an amino group (nh2) and a carboxyl group (cooh) and a hydrogen atom. Twenty common amino acid with featured based on side group of r . *r being any chemical group: nonpolar amino acids, uncharged polar amino acids, charged amino acids. When discussing protein structure, amino acids are referred to as residues.

Related Questions

BIOL 110 Principles of Biology

1.Describe the structure of a plasma membrane.

2.Define an amphipathic molecule and give an example.

3.Explain the difference between integral and peripheral proteins.

4.Describe the fluid-mosaic model of a membrane.

5.Identify and discuss the function of proteins located in the plasma membrane.

6.Explain the difference between glycoproteins and glycolipids.

7.Why can carbon form chemical bonds with so many elements?

8.Explain the meaning of concentration gradient as it pertains to movement of substances into and out of cells.

9.Explain diffusion and osmosis.

10.What molecule is thought to facilitate the movement of water molecules through a plasma membrane?

11.Explain the difference between active and passive transport across the plasma membrane. Provide examples that occur in the human body.

12.Explain the impact to a cell if placed in a hypertonic solution; include a definition of hypertonic solution and why the change occurs.

13.Identify a similarity and difference between facilitated transport and active transport. Do not state that both move substances across the membrane.

14.Explain the sodium-potassium pump and identify the type of membrane protein involved.

15.Identify and explain the process used by cells to secrete substances.

16.Explain the composition of a plant cell wall and how it differs from the cell wall of a prokaryotic cell.

17.Explain the plasmodesmata and identify the kingdom in which they are found.

18.Define energy and identify the two basic forms of energy.

19.Define entropy.

20.Define metabolism.

21.Explain the difference between exergonic and endergonic reactions.

22.What are coupled reactions and what roles can ATP serve in these reactions?

23.Explain the difference between oxidation and reduction reactions.

24.What is energy of activation?

25.What factors affect the speed of enzymatic reactions?

26.What is an electron transport chain?

27.What occurs at the active site of an enzyme?

28.Define enzymatic inhibition.

29.Define chemiosmosis.

30.Define vitamins and identify their function.

Protein Structure

a.Different function of proteins and examples:

b. Protein building blocks:

1. atomic composition of building block:

2. "parts" or "functional groups" of the building block:

c. Importance of side chain (R group):

d. Hydrophobic amino acids characteristics:

e. Hydrophilic amino acids characteristics:

f. Charged amino acids characteristics

Copy and complete the table below regarding the characteristics and which groups in the polypeptide interact together at each structural level of the protein.

	characteristics	groups interacting
Primary structure
Secondary structure
Tertiary structure
Quartenary structure

Value: 2

Choose the correct statement(s). You may choose more than one answer.

[mark all correct answers]
a. Proteins are the building blocks of amino acids.

b. Enzymes are a type of protein.

c. Quartenary structure consists of two or more polypeptide chains interacting.

d. Amino acids are made of carbon, hydrogen, nitrogen and phosphorus.

e. The primary structure of a protein is formed due to the interaction of side groups.

Value: 3

Put the following statements regarding the structural levels of a protein formation in the correct order.

Below is a sequence of events. Place them in the order they should occur, number 1 being the first item. Select the step number from the drop down next to each item.

Items to order:

1. Individual amino acids are bonded together via peptide bonds.

2. Two or more polypeptide chains interact via bonds.

3. Hydrogen bonds form between neighboring amino acids within a polypeptide chain allowing the chain to coil or form pleated sheets.

4. Side groups (R) of the individual amino acids interact with each other allowing the protein to assume its three dimensional shape.

Value:4

Put the following statements regarding the structural levels of a protein formation in the correct order

Individual amino acids are bonded together via peptide bonds.	1 2 3 4
Two or more polypeptide chains interact via bonds.	1 2 3 4
Hydrogen bonds form between neighboring amino acids within a polypeptide chain allowing the chain to coil or form pleated sheets.	1 2 3 4
Side groups (R) of the individual amino acids interact with each other allowing the protein to assume its three dimensional shape.	1 2 3 4

Value: 5

Hydrophobic amino acids will be found _______________.

a. In the interior (inner core) of a protein, away from the watery environment.

b. in the interior of a plasma membrane.

c. Both A and B

d. Neither

Value: 6

A protein's function is defined by ____________.

a. enzymatic reactions

b. it's shape.

c. chain of nucleotides.

d. the presence of carbon and hydrogen.

Value: 7

Which of the following is NOT considered a protein function?

a. transport of substances across membrane

b. enzymatic reactions

c. provides structural support

d. carries genetic information

Biology 1002B Lecture Notes - Lecture 3: Sulfide, Heme, Beta Sheet

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