Chemical nature of cells and biomechanics process in cells (chapter 1 and 3)

Question 1

Are proteins INORGANIC or ORGANIC?

Answer 1

ORGANIC

Question 2

What compounds are proteins made of?

Answer 2

C (carbon) H (hydrogen) O (oxygen)

Question 3

What is the monomer of proteins?

Answer 3

AMINO ACIDS

Question 4

How many naturally occurring amino acids are there?

Answer 4

20

Question 5

What does the order of the amino acids determine?

Answer 5

the structure of the protein

Question 6

What does the structure of the protein determine?

Answer 6

the function

Question 7

As soon as i see the ‘R’ variable i know its?

Answer 7

An Amino Acid

Question 8

R= And describe

Answer 8

Variable group This is a group compound that have variations in structure to give each amino acid a distinct characteristic.

Question 9

What do amino acids join together by?

Answer 9

CONDENSATION GRADIENT

Question 10

What bond is created by the condensation gradient?

Answer 10

PEPTIDE BOND

Question 11

What does two amino acids form?

Answer 11

A dipeptide

Question 12

What does many amino acids form?

Answer 12

A polypeptide

Question 13

How many types of protein structures are there? Name them

Answer 13

4. 1. Primary Protein Structure (1 degree) 2. Secondary Protein Structure (2 degree) 3. Tertiary Protein Structure (3 degree) 4. Quaternary Protein Structure (4 degree)

Question 14

Describe the primary protein structure

Answer 14

Strings of hundreds of amino acids link together with peptide bonds to form molecules called polypeptide chains.

Question 15

Describe the secondary protein structure

Answer 15

Polypeptide chains become folded depending on the attraction and repulsion properties between the various amino acids. There are 2 common forms of secondary structures: Alpa helix and Beta pleated sheets secondary structures are maintained by hydrogen bonds between CO+NH groups. The bonds are weak but strong enough to keep specific shape

Question 16

Difference between Alpha helix and Beta pleated sheets?

Answer 16

Alpha is curled/circular Beta is flat sharp angles

Question 17

Describe the tertiary protein structure

Answer 17

Formed by folding secondary protein structures. the folded proteins are held together by stronger sulphide compounds called DISULPHIDE BRIDGES. Weak IONIC and HYDROGEN bonds are also used to SPECIFIC structures. These types of proteins form GLOBULAR PROTEINS.

Question 18

describe the quaternary protein structure

Answer 18

By combining both tertiary and secondary structures, large complex proteins can be formed and are known as QUATERNARY PROTEINS. Example: Haemoglobin Some large proteins will also contain ‘non protein’ compounds, known as prosthetic groups.

Question 19

2 functional proteins

Answer 19

Globular proteins Fibrous proteins

Question 20

Describe globular

Answer 20

• easily water soluble - tertiary structure critical to function - polypeptide chains folded into a spherical (3 dimensional) shape - Enzymes: catalysts - Hormones: Insulin - Haemoglobin: Blood - Antibodies: immunity

Question 21

Describe Fibrous

Answer 21

• water insoluble - physically very tough: can be stretched or bent - Parallel polypeptide chains in long fibres or sheets - collagen found in cartilage, bones, tendons - Myosin: contractile in muscle - Keratin: nails and hair

Question 22

Enzymes are?

Answer 22

molecules that act as catalysts to speed up biological reactions

Question 23

Active site is made up of?

Answer 23

folding amino acids (globular)

Question 24

Are enzymes consumed during biological reaction?

Answer 24

no

Question 25

What is the compound on which an enzyme reacts?

Answer 25

The substrate

Question 26

Enzyme + Substrate --\> enzyme substrate complex --\> enzyme product complex --\> enzyme + product

Answer 26

amylase (enzyme) + amylopectin (polysacch) --\> amylase amylopectin complex --\> amylase maltose complex --\> amylase + maltose (enzyme and product)

Question 27

What are the two theories for enzyme action?

Answer 27

Lock and key theory Induced fit model

Question 28

Induced fit model description

Answer 28

the enzyme or the reactant (substrate) change their shape a little bit

Question 29

Why are enzymes able to speed up chemical reactions?

Answer 29

Because they are able to lower the activation energy requires to a reaction occur

Question 30

Activation energy definition

Answer 30

Is the amount of energy required to initiate a chemical reaction ie. break apart or join together chemical compounds by reducing the amount of energy required to initiate a chemical reaction, the reaction is sped up but the same outcome occurs.

Question 31

Enzyme activation graph

Answer 31

Enzyme activation graph

Question 32

what does a catabolic reaction involve?

Answer 32

The breakdown of larger molecules into smaller components with the release of energy. (they are exergonic)

Question 33

Enzymes involved in catabolic reactions can cause?

Answer 33

A single substrate molecule to be drawn into the active site.

Question 34

what does an anobolic reaction invlove?

Answer 34

smaller molecules to be joined together to form larger ones.

Question 35

Metabolic pathways:

Question 36

Feedback inhibition

Answer 36

1. A ------------\> B -------------\> C -------------\> D

Question 37

What are inhibiters?

Question 38

Competetive inhibiters?

Question 39

Non competitive inhibiters?

Answer 39

Will fit into a different part of the enzyme and change the shape of the enzyme. This causes the active site to chnage shape. Allosteric: used to describe position for where the non competitive inhibiter goes in.