Bio 183 Lect 1 (Test 1)

Front 1

Macromolecules that are fundamental to life:

Back 1

Lipid or fat
Protein
Carbohydrate
Nucleic acids

Front 2

Hemoglobin is a protein that means it is assembled from ____, it has ____ separate ____. It is a ____ based molecule.

Back 2

amino acids
4
subunits
carbon

Front 3

Hemoglobin
The weird red stuff are ____ subunits.
In the very center of each ____ is iron.
This molecule can hold onto ____ in certain metabolic conditions and let go of ____ under other certain metabolic conditions.

Back 3

heme
heme disc
oxygen
oxygen

Front 4

As we breathe in oxygen gets bound to ____.
4 molecules of oxygen gas bind on covalently to the ____ in each of the 4 subunits in the ____.

Back 4

hemoglobin
iron
hemoglobin

Front 5

At the capillaries, metabolic conditions shift so that the oxygen disassociates from the ____.

The empty ____ now picks up carbon dioxide, travels back to the alveoli and is released and you breathe it out.

Back 5

hemoglobin
hemoglobin

Front 6

____, 120 days, they break down.
Bone marrow cranks out ____, in the long bones.

Back 6

hemoglobin
hemoglobin/red blood cells

Front 7

Depending on which the atom it is bonding it can be ____ or ____.

Back 7

polar
non-polar

Front 8

In a ____ atom, the protons equal the electrons.

Back 8

neutral

Front 9

An atom is most stable when its outer shell is ____, so carbon is looking for ____ other electrons.

Back 9

filled
4

Front 10

Important feature of covalent bonds -

Back 10

PEGS
Polar vs nonpolar
Structural isomers
Geometric isomers
Enantiomers

Front 11

____ - are electrons equally or unequally shared?

Back 11

Polar vs nonpolar

Front 12

____ - two molecules may have the same number of atoms but they are differently arranged

Back 12

Structural isomers

Front 13

____ - when carbon is anchored by a double bond, where to other atoms reside in relation to the double bond?

Back 13

Geometric isomers

Front 14

____ - since 4 different atoms can bond with carbon, they can appear in either a "right" or a "left" handed arrangement.

Back 14

Enantiomers

Front 15

Key feature of the ____ atom, 4 electrons in the outer or valence shell.

Back 15

carbon

Front 16

Macromolecules that are fundamental to life =

Back 16

Major classes of organic molecules

Front 17

____ - electrons are equally shared, equal electro negativity both sides

Back 17

nonpolar

Front 18

In a ____ arrangement with another atom the electrons are equally shared between the two atoms. (they are "smack dab in the middle")

Back 18

nonpolar

Front 19

In a ____ arrangement there is a difference in electro negativity between the atoms.

Back 19

polar

Front 20

____ - electrons are not equally shared, not equal electro negativity both sides.

Back 20

polar

Front 21

In a ____ bond between oxygen and carbon the electrons are closer to the oxygen. The oxygen is more ____ and the carbon is more ____ in this example.

Back 21

polar
electronegative
electropositive

Front 22

c-h and c-c bonds are electrically ____ and ____

Back 22

neutral
nonpolar

Front 23

Oxygen is more electronegative than carbon; thus carbon oxygen bonds are ____ bonds.

Back 23

polar

Front 24

Alcohols have a ____ group.

Back 24

hydroxyl (-OH)

Front 25

____ have compliment (same type/amount) of atoms, but a different arrangement.

Back 25

Structural isomers

Front 26

____ - same side
____ - opposite side

Back 26

cis
trans

Front 27

Will have a "kink" in the ____ arrangement because the two hydrogen's are "in each others" way and push apart.

Back 27

cis

Front 28

Typically in nature we see ____ fatty acid chains.

Back 28

cis-

Front 29

4 different groups surrounding a ____ carbon can arrange differently

Back 29

chiral

Front 30

____ = right handed
____ = left handed

Back 30

Dextrorotary
Levrorotary

Front 31

____ = blood "sugar"
It is the chief transport molecule for animals.

Back 31

glucose

Front 32

Galactose = same ____ formula as glucose (has a flipped oh and h group)

Back 32

structural

Front 33

Glucose
β vs α is an up versus down -OH group.
____ versus ____.
We do not really see linear form in nature, think ring structure.

Back 33

Glucose
starch
cellulose

Front 34

Amino -

Back 34

R-NH2, found in proteins

Front 35

Ketone -

Back 35

RCOR , steroids, and proteins

Front 36

Aldehyde -

Back 36

R(C=O)H, Acts like a base, proton acceptor

Front 37

Carboxyl -

Back 37

RCOOH, amino acids, fatty acids
Acts like an acid, proton donator

Front 38

Hydroxyl -

Back 38

ROH, alcohol, carbs, steroids, some amino acids

Front 39

Methyl -

Back 39

RCH3, may be attached to dna, carbs, proteins

Front 40

Phosphate,

Back 40

R-PO4 2-, nucleic acids, ATP, attached to amino acids

Front 41

Sulfhydryl -

Back 41

R-SH, proteins that contain the amino acid cysteine

Front 42

Sulfhydryl - ____ like the hydroxyl arrangement.

Back 42

polar

Front 43

Carbohydrates

Back 43

ME
Mono, di and polysaccharides.
Energy yielding and structural molecules

Front 44

Fats

Back 44

MEH
Molecules characterized by long hydrocarbon chains and non polar nature.
Hydrophobic
Energy storage, cell membranes, sterols.

Front 45

Proteins

Back 45

MT
Molecules assembled from 20 amino acids.
The workhorse of the cell

Front 46

____
Assembled from 5 nucleotides, they hold the code for all proteins assembled by cells.

Back 46

Nucleic acids

Front 47

Simple carbohydrate = ____

Back 47

sugar

Front 48

Glucose + fructose = ____

Back 48

sucrose

Front 49

When you taste sugar you taste ____.

Back 49

readily available energy.

Front 50

Simple sugars are ___.

Back 50

mono or disaccharides.

Front 51

____- glucose and fructose

Back 51

Monosaccharide's

Front 52

____ - sucrose

Back 52

Disaccharide

Front 53

Carbs empirical formula

Back 53

CH2O

Front 54

Carbs have hydroxyl groups, these are ____ and so have a situation that the electrons spend more time orbiting the oxygen versus the hydrogen, this means that the hydrogen is positively charged.
The effect is it will readily interact with other ____ molecules (ex. ____)

Back 54

polar
polar
water

Front 55

Complex polymers assemble from ____.

Back 55

glucose

Front 56

____ is a polymer of glucose found in plants. (Food)
It has a bunch of ____ groups, that interact/branch with each other.

Back 56

starch
hydroxyl

Front 57

____ is a starch molecule found in animals. (____)

Back 57

Glycogen
animal starch

Front 58

____ is more highly branched than starch. (This is good because we have enzymes that chop off the last glucose on the chain)

Back 58

Glycogen

Front 59

____, Stored in liver and muscle. Can be catabolized (break down) when it is necessary.

Back 59

Glycogen

Front 60

____ - structural carbohydrate that provides that exoskeleton
Insectivores have enzyme to break down ____.

Back 60

Chitin
Chitin

Front 61

____ is used for structure by plants.
No branching, highly linearized rows.
Big difference ____ versus ___ linkages.
Bacteria etc in cows stomach can break down ____ linkages.

Back 61

Cellulose
alpha
beta
beta

Front 62

____ - often called lipids

Back 62

Fats

Front 63

____-
Large hydrophobic molecules usually characterized by a glycerol molecule and a hydrocarbon chain

Back 63

Fats

Front 64

____ molecules are also fats-
Sex hormones
Membrane molecules

Back 64

Sterol

Front 65

One of the most common -____
A 3 carbon backbone (glyclerol) with 3 fatty acid chains attached to it.

Back 65

triacylglycerol = triglyceride

Front 66

____ get packed with these triacylglycerols. Mainly saturated fats here.
Storage form for energy.

Back 66

Adiopocytes

Front 67

____ = carbon chain is filled up with hydrogens.

Back 67

Saturated

Front 68

____ = carbon chain is not full of hydrogens.

Back 68

Unsaturated

Front 69

____ will be solid at room temperature.

Back 69

Saturated

Front 70

Kinked fatty acids - _____ will not lie nice and flat next to each other, so
Will be liquid at room temperature.

Back 70

(unsaturated)

Front 71

Unsaturated fats can be ___ or ____.

Back 71

monounsaturated or polyunsaturated

Front 72

____ - the primary/chief constituent/component of cell membranes.

Back 72

Phospholipid

Front 73

____ is composed of a glycerol backbone, 2 fatty acids, and a phosphate and a head molecule on the phosphate group.

Back 73

Phospholipid

Front 74

____ - A polar head (hydrophilic) and a nonpolar tail (hydrophobic)
The polar head operates at the aqueous outer or inner part of the cell membrane. The nonpolar tail acts as the barrier.

Back 74

Phospholipid

Front 75

Some cell membranes are more fluid than others, that fluidity is related to the degree of ____ of those fatty acids.

Back 75

unsaturation

Front 76

Sex hormones are ____/____ molecules that are considered fats because they are nonpolar and fairly large.

Back 76

sterol
steroid

Front 77

Sterols - or steroids
Example -

Back 77

estradiol and testosterone.

Front 78

____ - male and female differ colorwise, a sex characteristic driven by the sex hormone

Back 78

Dichromatic

Front 79

____ - also a fat, it is found in cell membranes

Back 79

Cholesterol

Front 80

____ gets a fatty acid attached to it and hangs out in the cell membrane. This helps the membrane cope with ____ changes. It also assists in the level of ____ that that membrane has.

Back 80

Cholesterol
temperature
fluidity

Front 81

Carbs - all share the same ratio ____

Back 81

CH2O

Front 82

carb types-

Back 82

SSCC
Sugars
Starches
Cellulose
chitin

Front 83

Starch types -

Back 83

plant starch
glycogen

Front 84

Fats (chars) -

Back 84

Large
Nonpolar
Hydrophobic

Front 85

Fat types -

Back 85

TFPS
Triacylglycerols (triglycerides)
Fatty acids
Phospholipids
Sterol molecules

Front 86

Each protein has a very specific ____ order.

Back 86

amino acid

Front 87

Highly complex, 20 different amino acids.

Back 87

proteins

Front 88

____ - are arranged in a linear chain polymer and joined together by peptide bonds

Back 88

Amino acids

Front 89

____ -
Macromolecules assembled from amino acids
Many metabolic roles in the cell.

Back 89

Proteins

Front 90

____ - a group with an amino group and an acid group!

Back 90

Amino acid

Front 91

____ pH, blood in body is approx 7.36.

Back 91

Physiological
7.36 (7.4)

Front 92

Amino Acids
Amino group can act as ____, carboxyl group as ____.

Back 92

bases
acids

Front 93

Amino Acids
The carbon in the middle is always the ____ carbon.

Back 93

alpha

Front 94

____ are assembled from amino acids!

Back 94

Proteins

Front 95

Amino acid has -

Back 95

R group
Carboxyl group
Amino group
Hydrogen

Front 96

____ have all kinds of functional roles.
____ are the workhorse of the cell.

Back 96

Proteins
Proteins

Front 97

____ - newest of the tastes, savory, think red wine, mushroom and meat.

Back 97

Umami

Front 98

____ - initiate movement

Back 98

Motor proteins

Front 99

____ - associated with immune system

Back 99

Defense proteins

Front 100

____ - help move stuff across lipid bilayer
Ex. Aquaporin, gatekeeper

Back 100

Transporters

Front 101

____ - move stuff around in a multicellular organism, ex hemoglobin

Back 101

Transport protein

Front 102

____ - supports and strengthens structures

Back 102

Structural protein

Front 103

____ - enzymes,

Back 103

Metabolic proteins

Front 104

Amino Acid General rules:

Back 104

Polar, no charge - have amide or hydroxyl group at the end (not tyrosine)
Polar, charged- a charge is at the end
Nonpolar - the rest of em

Front 105

____ = amino acid

Back 105

Peptide

Front 106

____ = a lot of amino acids

Back 106

Polypeptide

Front 107

Always have a start point and an end point.
____ side is always the beginning
and numbering starts here.
____ and ____.

Back 107

amino
N-terminus
C-terminus

Front 108

Proteins are assembled from ____
20 ____
Each protein has a specific amount and number of ____ in a particular order.

Back 108

amino acids
amino acids
amino acids

Front 109

Structural Levels of Protein
____ - the amino acid sequence

Back 109

Primary

Front 110

Structural Levels of Protein
____ - shape caused by bonding along the backbone,
Non-covalent interactions

Back 110

Secondary

Front 111

Structural Levels of Protein
____ - shape caused by bonding of R-groups
Can be covalent

Back 111

Tertiary

Front 112

Structural Levels of Protein
____ - shape caused by bonding of two distinct amino acid chains. R groups interacting.
Can be covalent

Back 112

Quaternary

Front 113

Secondary structure-

Back 113

α helix
β pleated sheet

Front 114

Structural Levels of Protein
____ - whole thing coils

Back 114

Tertiary

Front 115

Structural Levels of Protein
____ - two or more polypeptides.

Back 115

Quaternary

Front 116

All the structural levels are important, but cant do anything without the ___.

Back 116

primary level
no foundation to build upon

Front 117

One amino acid change is a ____.

Back 117

point mutation.

Front 118

Ex. Normal hemoglobin a sickle hemoglobin. The only difference is ____. This causes the red blood cell to form that sickle shape.

Back 118

one amino acid change

Front 119

____ = break something down

Back 119

Catabolize

Front 120

____, a protein that catbolizes rna

Back 120

Ribonuclease

Front 121

5 amino acid forces:

Back 121

Hydrogen bonds
Ionic Bond
Hydrophobic effect
Van Der Waals forces
Disulfide bridge.

Front 122

(Geckos can walk on glass due to ____ forces)

Back 122

van der waals

Front 123

____ - a covalent bond forms between 2 cysteine side chains.

Back 123

Disulfide bridge

Front 124

____ - Attractive forces occur between atoms that are optimal distances apart

Back 124

Van Der Waals forces

Front 125

____ - nonpolar amino acids in the center of the protein avoid contact with water

Back 125

Hydrophobic effect

Front 126

____ - bonds form between oppositely charged side chains

Back 126

Ionic bond

Front 127

____ - bonds form between atoms in the polypeptide backbone and between atoms in different side chains

Back 127

Hydrogen bonds

Front 128

Nucleic acids - ____ and ____
They hold the ____.

Back 128

RNA
DNA
genetic code

Front 129

____ is a "library", of all the proteins.
____ assists in taking the information from the library and creating a protein.

Back 129

DNA
RNA

Front 130

Nucleic acids (Key Features..)-

Back 130

Assembled from nucleotides
RNA and DNA
Hold genetic code
Assist in protein synthesis

Front 131

Dna, has been deoxy'd that is it does not have the ____ group that is present on RNA. (this is difference between a ribonucleotide and a deoxyribonucleotide)
They both have a 5 carbon sugar, a phosphate group and a nitrogenous base.

Back 131

hydroxyl

Front 132

The ____ group is the anchor/backbone of the molecule (DNA/RNA).

Back 132

phosphate

Front 133

Double stranded helix,
The interactions is non-covalent hydrogen bonds between these bases.
The two strands run against each other.

Back 133

DNA

Front 134

Nucleic acids -

Back 134

GARD
Assembled from 5 nucleotides (T/U, A , G, C)
RNA and DNA
DNA strands are antiparallel to one another.
Genetic code and protein synthesis.

Front 135

Proteins -

Back 135

MC4A
Assembled from 20 amino acids
4 structural levels
Covalent and noncovalent interactions stabilize structure
Many functional roles