Bsc 2010 Exam One (Chapters 1-6)

Front 1

Properties of living things?

Back 1

Order, regulation, energy processing, growth & development, reproduction, response to the environment, evolutionary adaptation

Hint 1

7 things

Front 2

Difference between eukaryotic and prokaryotic cells?

Back 2

The presence of membrane-bound organelles

Front 3

Biological diversity; how do we explain difference among organisms?

Back 3

The accumulation of heritable changes (variation in DNA sequence)

Front 4

What is DNA? Where does variation in DNA sequence come from?

Back 4

- Units of inheritance that transmit info from parents & offspring

- Controls development & maintenance of organism

Front 5

What is a genome? A gene?

Back 5

- Genetic material of an organism; complete complement of an organism's genes along with its noncoding nucleic acid sequence

- Unit of heredity info consisting of a specific nucleotide sequence in DNA

Front 6

What is a genotype? What is phenotype?

Back 6

- Genetic makeup (set of alleles, DNA sequence)

- Physical expression of genes

Front 7

Element

Back 7

Substance that cannot be broken down physically

Front 8

Compound

Back 8

Consists of 2 or more elements

Front 9

Atom

Back 9

Smallest unit that contains the property of an element

Front 10

Neutron

Back 10

In nucleus, subatomic particle w/o a charge

Front 11

Proton

Back 11

In nucleus, subatomic particle with + charge

Front 12

Electron

Back 12

Negative charge, orbits around nucleus,

Front 13

Atomic #

Back 13

# of protons (# of electrons = # of protons)

Front 14

Mass #

Back 14

Sum of # protons & electrons

Front 15

Atomic mass

Back 15

How much atom mass

Front 16

What 4 elements make 96% of living matter?

Back 16

CHON (Carbon, hydrogen, oxygen, nitrogen)

Front 17

What makes up the other 4% of living matter?

Back 17

Ca, P, K, S, Na, Cl, Mg

Front 18

What is iodine used for the body?

Back 18

- Production of thyroid hormone

- Regulate growth & metabolism

- Basal metabolic rate, protein synthesis, bone growth, neural maturation

Front 19

How do arsenic, lead, & mercury affect the body?

Back 19

- Affects energy production in mitochondria; apoptosis; lead to cancer, developmental issues, neural issues, death

- Disrupts function by causing by causing production of reactive oxygen species (ROS), more dangerous for children

- Disrupt function by causing ROS; destroys protein inside the cells

Front 20

What is an isotope?

Back 20

Different forms of the same element; difference is by neutrons

Hint 20

Not to be confused with isomer

Front 21

How do we exploit radioactive isotopes?

Back 21

-Unstable forms of an element; have a tendency to lose particles

- Used in fossil dating, tracers, diagnostics & imaging

Front 22

The importance of electrons?

Back 22

- They store potential energy

- They bring about chemical bonding

- When a molecule is being created, the electron that's doing it

Front 23

The different bonds of molecules?

Back 23

- Covalent- (strong bonds, interaction between electrons)

- Non- covalent- (weak, bindings to be reversible)

Front 24

Different non-covalent bonds?

Back 24

- Ionic- highly electronegative molecule takes an electron from another molecule

- Hydrogen- allows different molecules to interact w/ each other; oxygen & hydrogen

- Van de Waals- Very short distances any two atoms show a weak bonding interaction

- Hydrophobic- Forced together minimize the disruptive effects of hydrogen bonds

Hint 24

HIVH (acronym)

Front 25

Why are non-covalent bonds used in many molecule interactions?

Back 25

Shows the feature of molecules (shape of molecules)

Front 26

Why is molecule shape important? What does it determine?

Back 26

- Shape is determined by where the atom's electron orbitals are positioned

- Shape determines function

Front 27

What is meant by equilibrium?

Back 27

When the rate of one reaction is equal to the other

Front 28

What are the 4 macromolecules?

Back 28

- Protein

- Nucleic acids

- Carbohydrates

- Lipds

Hint 28

PNCL (acronym)

Park "N" climb left

Front 29

What are the 4 ways carbon skeletons can vary?

Back 29

- Length

- Branching

- Presence of rings

- Double bond position

Front 30

What hydrophobic and hydrophilic mean and what determines each?

Back 30

- Substances that are nonionic & non polar; no water affinity

- Has affinity for water

Front 31

What are isomers? Will their function be the same?

Back 31

- Compounds wight the same molecular formula, but different structures

- No, since they have different properties

Hint 31

Not to be confused with isotopes

Front 32

Types of isomers?

Back 32

- Structural- differ in the covalent arrangements of atoms

- Cis-trans- differ in the spatial arrangements due to inflexibility of double bonds

-Enantiomers- mirror images of each other & differ in shape due to presence of an asymmetric carbon

Front 33

Functional groups & their roles

Back 33

- Provide function

1. Provide shape & structure

2. Reactivity

3. Solubility

Front 34

ID functional groups

Back 34

- Hydroxyl group (-OH)

- Carboxyl group (-COOH)

- Sulfhydral group (-SH)

- Methyl group (-CH3)

- Carbonyl group (-C=O)

- Amino group (-NH2)

- Phosphate group (-OPO3 2-)

Front 35

What is a polymer?

Back 35

Long molecule consisting of many similar building blocks linked by covalent bonds

Front 36

Dehydration vs. Hydrolysis

Back 36

- Loss of a water molecule; two molecules covalently bonded to each other

- Reverse of the dehydration reaction; break bonds using water

Front 37

Classification of sugars

Back 37

- Alpha glucose (same side)

- Beta glucose (opposite side)

Front 38

Roles of polysaccharides?

Back 38

- Storage material

- Building material for structures that protect the cell or whole organism

Front 39

What are lipids?

Back 39

- Diverse group of hydrophobic molecules

- Mix poorly w/ water

- Large biological molecules that doesn't include true polymers

Front 40

What is a triglyceride?

Back 40

- Three fatty acids joined to glycerol by an esther linkage

- Covalent bonds

Front 41

Saturated vs. Unsaturated

Back 41

- No double bonds between carbon atoms composing a chain; many hydrogen atoms of possible are bonded; w/ hydrogen

- One or more double bonds; one fewer hydrogen atom on each double- bonded carbon; cis double bonds; kink in hydrocarbon chain

Front 42

Functions of fats (triglycerides, phospholipids)

Back 42

- Energy storage; store long term food in reserves in adipose cells

Front 43

Membrane structure & cholesterol

Back 43

- Steroids

- Four fused rings

- Distinguished by the particular chemical groups attached to this ensemble of rings

Front 44

Protein structure

Back 44

Four levels: - Primary- protein is its sequence of amino acids

- Secondary- A coil called alpha helix and a folded structure called a beta pleated sheet

- Tertiary- Overall shape of a polypeptide; functional 3-D shape

- Quaternary- When 2 or more polpeptide chains form one macromolecule

Front 45

Amino acid structure; classification of amino acids

Back 45

- Organic molecule that has both an amino group and a carboxyl group

- Four classes: Hydrophobic (non polar side chains), hydrophilic (polar side chains), acidic (negatively charge), basic (positively charge)

Front 46

What is a peptide bond?

Back 46

Covalent bond between the carboxyl group on one amino acid and the amino group on another; formed by a dehydration reaction

- Length depends on protein

- Sequence depends what the protein will be

Front 47

What reactions make or break peptide bonds?

Back 47

- Broken by hydrolysis, made by dehydration

Front 48

Sequence, structure, and function of peptide relationship

Back 48

- Determines what the protein will be

- Side chains create function

Front 49

Physical properties that determine protein structure?

Back 49

- Physical & chemical conditions

- Alterations in pH, salt concentration, temperature, pressure, or other environmental factors

Front 50

What is denaturation

Back 50

Process which a protein loses its native shape due to the disruption of weak chemical bonds & interactions, thereby becoming biologically inactive

- In DNA it is the separation of the two strands of the double helix

Front 51

What is a chaperonin and what does it do?

Back 51

- Protein molecules that assist in the proper folding of other proteins

- Keep the polypeptide segregated from the bad influences in the cytoplasmic environment while it folds spontaneously

Front 52

Define nucleic acid, nucleotide, & gene

Back 52

- Polymers made of monomers & two types= DNA & RNA

- Composed of three parts: phosphate group, sugar group, & nitrogenous base

- Gene- unit of inheritance

Front 53

Difference between DNA & RNA

Back 53

- DNA: forms double helix, backbones run antiparallel, strings move in opposite direction, A=T; G(triple bond)C

- RNA: single stranded, ribose instead of deoxyribose, G(triple bond)C; A=U

Front 54

Know purines and pyramidines

Back 54

- Large, w/ a six-membered ring fused to a fire-membered ring; adenine (A) and guanine (G)

- One six-membered ring of carbon & nitrogen atoms; cytosine (C), thymine (T), and uracil (U)

Front 55

What is a phosphodiester linkage?

Back 55

- In DNA & RNA, linkage between 3' carbon atoms of one sugar molecule & 5' carbonator of another; deoxyribose in DNA and ribose in RNA

- Strong covalent bond

Front 56

What does antiparallel mean?

Back 56

Two sugar-phosphate backbones run in opposite 5'->3' directions from each other

Front 57

What is complimentary base pairing?

Back 57

- A base sequence & the other strand is the predictable counterpart of the other

Hint 57

ex. 5'- AGGTCCG-3'

3'- TCCAGGC-5'

Front 58

Role of nucleic acids?

Back 58

- Allow for transmission of inheritable traits to offspring

-DNA provides directions for its own replication

~unique emergent property

Front 59

What is central dogma?

Back 59

- Two-step process, transcription and translation, by which the info in genes flows into proteins: DNA->RNA->Protein

- Transcription of an RNA copy of a segment of DNA

Front 60

What feature do ALL cells have?

Back 60

Cell membrane, cytosol, DNA, & ribosomes

Front 61

What does surface area-to-volume ratio place a limit on the size of cells

Back 61

*refer to study guide

Front 62

Explain the structure & function of the nucleus

Back 62

- Contains most of the cell genes & most conspicuous organelle

- Nuclear envelope- Double membrane structure outer membrane continuous w/ ER

- Pore- regulate large molecules that move in and out

- Nuclear lamina- strengthens the membrane

Front 63

What do ribosomes do in cells? What types of macromolecules are ribosomes constructed from? Difference between free & bound ribosomes?

Back 63

- Responsible for creating protein; outside of ER or nuclear envelope (bound ribosomes)

- Ribosomal RNA & Protein/polypeptides

- Free ribosomes: Suspended in the cytosol; most proteins made function within the cytosol

- Bound ribosomes: Attached to the outside of the ER or nuclear envelope; make proteins that are destined for insertion into membranes or to export from cell like secretion

Front 64

List all organelles whose membranes are considered part of the endomembrane system. What functions does the EMS serve for the cell?

Back 64

- Nuclear envelope; endoplasmic reticulum; golgi apparatus; lysomes; perxisomes; plasm membrane

- Regulates protein traffic and performs metabolic functions in the cell

Front 65

Summarize the structure & function of the RER and the golgi apparatus

Back 65

- Closest to nucleus; covered w/ ribosomes; membrane factory for the cell; grow in place by adding membrane proteins & phospholipids to its membrane; makes membrane phospholipids

- Has cis (largest outer radius) & trans (closest to cell membrane); modifies products of the ER; manufactures certain macromolecules; protein modification; creation of polysaccharides- modifications of polysaccharides

Front 66

Describe functions performed by SER

Back 66

Farther from nucleus; create lipids (lipid synthesis); detoxification; metabolize certain amount of carbs; calcium storage

Front 67

Functions of lysosomes in the cell

Back 67

- Phagocytosis- takes things from external environment (digesting food)

- Autophagy- when larger parts of cell wear out, recycles its nutrients to make new organelles

- fuses with the food vacuole & digests the molecules

Front 68

Summarize the functions of each of the 3 types of vacuoles- central, contractile, and food

Back 68

- Central: major role in the growth of plant cells; holds reserves of important organic compounds; disposal site for metabolic by products; protects against predators

- Food vacuole: contains food from outside of the cell; formed by phagocytosis; forms by budding in from the cell membrane

- Contractile: Pumps excess water out of the cell; maintaining a suitable concentration of ions and molecules inside the cell; offsets osmosis by pumping water out of the cell