Lecture Exam 1: Chapter 2B Cards

Front 1

Define organic with respect to molecules. Give examples

Back 1

Produced by living things and contains C-H bonds.
Ex: amino acids, sugars

Front 2

Define inorganic molecule.
Give examples

Back 2

Produced by non-living things or by humans in a lab and does NOT contain C-H bonds.
Ex: water, oxygen,salt, carbon dioxide

Front 3

Describe water as a molecule and why is it central to life?

Back 3

It is a Polar molecule and participates in hydrogen bonding, It is a liquid,is a universal solvent, the most abundant compound in the body, and provides cushioning.

Front 4

What is the role of oxygen in the human body? Which chemical properties of oxygen contribute to the suitability of oxygen for this role?

Back 4

Reduction of oxygen to water increases the energy that we can use form metabolizing sugars and fats. Forms free-radicals!
Reactive: so it can form the free radicals.
Good electron acceptor for metabolic reactions.

Front 5

Define Salt, Give an example, and why is it important?

Back 5

An ionic compound produced by reacting an acid with a base. Ex: NaCl
It is important for the control of water homeostasis, the maintenance of pH, muscle contractions, nerve transmission, and cell signaling.

Front 6

Define pH and the numerical scale associated with acidic, basic, and neutral levels.

Back 6

The pH scale measures how acidic or basic a substance is. The pH scale ranges from 0 to 14. A pH of 7 is neutral. A pH less than 7 is acidic, and a pH of more than 7 is basic.

Front 7

What is the difference between a strong acid/base and a weak one?

Back 7

Strong dissolve completely, and weak only partially dissolve.

Front 8

What is a buffer?

Back 8

A buffer stabolizes the pH of a solution because it releases both H+ and OH- depending on what is needed to keep the solution neutral. Ex: water

Front 9

How can carbon dioxide serve as a buffer?

Back 9

It turns into carbonic acid that can increase or decrease the pH of blood in the body.

Front 10

What is the relationship between monomers and polymers?

Back 10

Monomers combine to form polymers.

Front 11

Define Dehydration Synthesis and give example

Back 11

A + B = C
Building something up or linking molecules by taking water out(dehydrate).
Ex: Glucose to Maltose or Alcohol to Ether

Front 12

Define Hydrolysis and give an example

Back 12

C = A + B
Breaking bonds between molecules by adding water (hydrate)
Ex: Peptides to Amino acids

Front 13

What is a carbohydrate? Identify monomeric forms and polymer forms. Know the general molecular structure.

Back 13

It consists of 1:2:1 ratio of Carbon: Hydrogen: Oxygen and it forms 'Sugar'. Glucose (monomerir form), Sucrose and Cellulose (polymer form). Structure of a carbon 'backbone' with a hydroxyl group and a Carbonyl group, and can also form a ring structure.

Front 14

Describe the general chemical properties of lipids

Back 14

Hydrophobic (fear water), Non Polar, Mainly C and H atoms.

Front 15

Basic structure of a fatty acid

Back 15

Basic formula =(CH2)n
Long chains of carbon with hydrogens and an OH at the end to make them an acid. Composed part of triglycerides and phospholipids.

Front 16

Structure of a Triglyceride

Back 16

Composed of 3 (tri) fatty acids; (2 saturated) and (1 unsaturated) + glycerol 'backbone'

Front 17

Structure of a Phospholipid

Back 17

Phosphorous-containing a head group + 2 fatty acids on a glycerol backbone. This makes a polar head (positively charged) and a hydrophobic tail. Ex: the cell membrane

Front 18

Structure of a Steroid

Back 18

3 Six-point rings and 1 five-point ring all attached together to form a hydrophobic molecule.

Front 19

Identify some biological roles for cholesterol.

Back 19

Regulated fluidity of cellular membranes, produces all other steroid hormones, is the precursor to bile acids and vitamin D, and is critical to LIVE!

Front 20

Describe the general structure of amino acids and how they form proteins

Back 20

The 'backbone' of an amino acid has an amino group, a carboxyl group and a R group (that differentiates what kind of amino acid it is). Peptide bond (protein) forms by dehydration of 2 amino acids.

Front 21

Primary Structure

Back 21

Predicts the ORDER of the amino acids blocks.

Front 22

Secondary Structure

Back 22

Maintains the SHAPE
1. Helix (DNA)
2. Pleated sheet

Front 23

Tertiary Structure

Back 23

Created a 3-D shape for more space.

Front 24

Chaperones

Back 24

Proteins in cells that help ensure that the secondary and tertiary structure is correct,

Front 25

Quarternary Struture

Back 25

How proteins associate with one another. (usually 4)

Front 26

What are the general roles for proteins in the body?

Back 26

Storage, Defense, Transport, Signaling, and making Enzymes.

Front 27

What is an enzyme and what does it do?

Back 27

It is a catalyst (speeds up a reaction) that is NOT used up after the reaction is completed.

Front 28

Name the 5 Nucleobases

Back 28

Adenine
Guanine
Cytosine
Thymine (DNA)
Uracil(RNA)

Front 29

Name the 2 main types of polynucleotides and their roles

Back 29

1. DNA (Deoxyribose): genetic material that forms C, G, A, T and is DOUBLE stranded.
2. RNA (Ribose): Protein coding that forms C, G, A, U and is SINGLE stranded.

Front 30

Describe the general structure of ATP and its role in the cell.

Back 30

It has 3 phosphate groups, a sugar, and a adenine (base). It produces energy by means of hydrolysis.