Cell And Molecular Biology Exam 1

Front 1

characteristics of living things?

Back 1

1. take in and use energy
2. sense and respond to changes in env.
3. grow and reproduce
4. consist of one or more cells
5. maintain homeostasis

Front 2

Robert Hooke

Back 2

coined the word "cells"; examined cork

Front 3

Leeuwenhoek

Back 3

protozoa and bacteria

Front 4

Brown

Back 4

discovery of the nucleus

Front 5

Schleiden and Schwann

Back 5

cell theory

Front 6

Bacteria lack what?

Back 6

cell nucleus and cell organelles

Front 7

Karyon

Back 7

kernel or nucleus

Front 8

pro means what?

Back 8

before

Front 9

Eu means what?

Back 9

well or true

Front 10

organisms whose cells have a nucleus

Back 10

eukaryotes

Front 11

all cells contain ___ copies of DNA

Back 11

identical

Front 12

How are cells different from each other?

Back 12

they express different genes

Front 13

All differentiated cell types are generated during _____ _____ from a ____ _____ ___ cell

Back 13

embryonic development; single fertilized egg cell

Front 14

genome

Back 14

entire genetic information in a cell's DNA

Front 15

DNA provides what to the cell?

Back 15

genetic program that instructs the cell how to function and how to grow into an organism

Front 16

species that live in soil or make us ill

Back 16

eubacteria

Front 17

found in harsh environments

Back 17

archaebacteria

Front 18

controls movement of subs. in and out of cell, maintains cytoplasmic comp, volume

Back 18

membrane

Front 19

master control center containing DNA instructions for cell building, structure and function

Back 19

nucleus

Front 20

double membrane system that keeps water soluble substances from moving freely in and out of the nucleus

Back 20

nuclear envelope

Front 21

all the cellular parts, particles and semi-fluid substances enclosed by plasma membrane except for nucleus

Back 21

cytoplasm

Front 22

fluid portion of nucleus interior

Back 22

nucleoplasm

Front 23

RNA and protein are combined to make subunits of ribosomes

Back 23

nucleolus

Front 24

assemble polypeptide chains

Back 24

ribosomes

Front 25

routes and modifies newly formed polypeptide chains

Back 25

ER

Front 26

modifies polypeptide chains into mature proteins, sorts and ships proteins and lipids for secretion or use inside cell

Back 26

golgi apparatus

Front 27

intracellular digestion, excretion, helps recycle material

Back 27

lysosome

Front 28

produce ATP

Back 28

mitochondria

Front 29

microfilaments, microtubules, and intermediate filaments that give shape to the cell, support cell and organize and move its internal components

Back 29

cytoskeleton

Front 30

hydrogen peroxide generated and degraded

Back 30

peroxisomes

Front 31

large green organelles found only in plants and algae

Back 31

chloroplast

Front 32

possess internal stacks of membranes containing the green pigment chlorophyll

Back 32

chloroplasts

Front 33

trap the energy of sun and use this to drive the manufacture of energy-rich sugar molecules

Back 33

chlorophyll

Front 34

contain their own DNA, reproduce by dividing in two and are thought to have evolved from bacteria

Back 34

chloroplasts

Front 35

rod-shaped bacterial cell that lives in the gut of humans and other vertebrates

Back 35

E. coli

Front 36

small weeds grown indoors, produces thousands of offspring per plant in 8-10 weeks

Back 36

arabidopsis thaliana

Front 37

used in classical study of genetics

Back 37

drosophila and c elegans

Front 38

chains of chemical subunits held end to end

Back 38

polymeric molecules

Front 39

combination of elements

Back 39

matter

Front 40

smallest particle of an element that retains distinctive chemical properties

Back 40

atom

Front 41

atoms linked together in groups

Back 41

molecules

Front 42

hold atoms together in molecules

Back 42

chemical bonds

Front 43

donates electrons

Back 43

positively charged ion

Front 44

accepts electrons

Back 44

negatively charged ion

Front 45

share a pair of electrons

Back 45

covalent bonds

Front 46

molecule held together by polar covalent bonds; has no net charge

Back 46

hydrogen bonding

Front 47

small and large carbon compounds

Back 47

organic molecules

Front 48

all other molecules including water

Back 48

inorganic

Front 49

functional groups:
OH
NH2
COOH
PO3-
CO
C=O

Back 49

hydroxyl
amino
carboxyl
phosphate
ketone
carbonyl

Front 50

four major families of organic molecules

Back 50

sugars
fatty acids
amino acids
nucleotides

Front 51

simplest sugars

Back 51

monosaccharides

Front 52

molecules with same formula but different structures

Back 52

isomers

Front 53

has central role as an energy source for cells

Back 53

glucose

Front 54

mirror-image pairs of molecules

Back 54

optical isomers

Front 55

polysaccharides

Back 55

glycogen, starch

Front 56

most abundant polysaccharide on earth

Back 56

cellulose

Front 57

linear polymer of N-acetyl glucosamine; makes up insect exoskeletons and fungal cell walls

Back 57

chitin

Front 58

smaller oligosaccharides are covalently linked to proteins

Back 58

glycoproteins

Front 59

fatty acid parts

Back 59

long hydrocarbon chain-hydrophobic
carboxylic acid group-hydrophilic

Front 60

both hydrophilic and hydrophobic

Back 60

amphipathic

Front 61

Why do organisms require a continual supply of energy to exist?

Back 61

because thy create order out of disorder inside their cells

Front 62

How is life is thermodynamically possible (even though it appears that living things defy the second law of thermodynamics)?

Back 62

cells in living things release heat to the environment and thereby increase disorder

Front 63

What does photosynthesis do?

Back 63

Convert light energy into heat energy and chemical bond energy

Front 64

Energetically favorable reaction

Back 64

glucose-1-P --> glucose 6-P
sucrose --> glucose + fructose
ATP --> ADP + P
glucose + O2 --> 6CO2 + H2O (respiration)
sucrose --> CO2 + H2O

Front 65

How does an enzyme speed up a reaction?

Back 65

It lowers the activation energy of a reaction.

Front 66

T/F. Reactions cannot be coupled without enzymes.

Back 66

True

Front 67

T/F The temperature increase required to speed up a reaction by an appreciable extent is often huge. Therefore, enzymes are more favorable to heat.

Back 67

True

Front 68

T/F Enzymes catalyze a limited number of reactions, while heat affects all the reactions in a cell.

Back 68

True

Front 69

T/F enzymes change the equilibrium of biochemical reactions.

Back 69

False

Front 70

What are energetically favorable reactions?

Back 70

Those that decrease the free energy of a system.

Front 71

What is a common means of providing energy to an energetically unfavorable reaction in a cell?

Back 71

coupling ATP hydrolysis (energetically favorable rxn) to the reaction

Front 72

the part of the amino acid group that determines its chemical properties

Back 72

R group

Front 73

positive delta G

Back 73

nonspontaneous; not energetically favorable

Front 74

negative delta G

Back 74

spontaneous; energetically favorable

Front 75

link amino acids together

Back 75

peptide bond

Front 76

also called polypeptides

Back 76

proteins

Front 77

consists of a backbone that supports different AA side chains

Back 77

polypeptide chains

Front 78

formed from the repeating sequence of the core atoms of the AA that form these chains

Back 78

polypeptide backbone

Front 79

give AA their unique properties

Back 79

side chains

Front 80

2 negatively charged AAs

Back 80

aspartic acid (D)
glutamic acid (E)

Front 81

3 positive AAs

Back 81

Arginine
Lysine
Histidine

Front 82

uncharged polar

Back 82

asparagine
glutamine
serine
threonine
tyrosine

Front 83

covalent bonds that link carbon atoms allow what?

Back 83

free rotation of the atoms they join

Front 84

weak noncovalent bonds are responsible for what?

Back 84

constraining the folded chain that forms within proteins

Front 85

hydrophobic forces help proteins fold

Back 85

conformations

Front 86

how is free energy is minimized

Back 86

a protein generally fold into a shape

Front 87

protein's final folded structure

Back 87

conformation

Front 88

How is conformation determined?

Back 88

by its energetic considerations

Front 89

treatment with solvents that disrupt the noncovalent interactions holding the folded chain

Back 89

denaturing proteins

Front 90

once solvent is removed, protein folds bock into original conformation

Back 90

renaturing

Front 91

a pair of a-helices wrapped around one another

Back 91

coiled coil

Front 92

assist with protein folding in living cells

Back 92

molecular chaperones

Front 93

prevent newly synthesized protein chains from associating with wrong partners

Back 93

chaperones

Front 94

the first folding pattern of proteins to be discovered

Back 94

a helix (keratin)

Front 95

found in fibroin in silk

Back 95

beta sheets

Front 96

folding occurs as a result of what?

Back 96

hydrogen bonds forming between N-H and C=O groups in the polypeptide backbone

Front 97

amino acid sequence

Back 97

primary structure

Front 98

folding in the protein; a helices beta sheets

Back 98

secondary structure

Front 99

3D conformation of entire polypeptide chain

Back 99

tertiary

Front 100

complete structure of one or more polypeptide chains

Back 100

quarternary

Front 101

any segment of the polypeptide chain that can fold independently in a compact, and stable structure

Back 101

protein domain

Front 102

any region on a protein's surface that interacts with another molecule through sets of noncovalent bonds

Back 102

binding sites

Front 103

the tight binding of two folded polypeptide chains that creates a larger protein molecules; each polypeptide chain in such a protein is called

Back 103

subunit

Front 104

subunits can pack to form what shapes

Back 104

filament, tube, spherical shell

Front 105

collagen, elastin

Back 105

fibrous