Abac Cell & Molecular Biology Chapter 2

Front 1

Covalent Bonds

Back 1

Bonds b/t atoms w/ shared pairs of electrons

Front 2

How many Kilocalories does it take to break a covalent bond?

Back 2

80-100 Kilocalories

Front 3

Electronegativity

Back 3

The atoms nucleus' attraction force of electrons

Front 4

Polar

Back 4

Opposing charges on a molecule in their on region.

Front 5

Nonpolar

Back 5

Molecules w/ the same charge equally distributed around the molecule

Front 6

Anions

Back 6

Have a negative

Front 7

Cations

Back 7

Have lost electrons

Front 8

Free radicals

Back 8

are unstable atoms or molecules w/ unpaired electrons

Front 9

Superoxide dismutase (SOD)

Back 9

is an enzyme that destroy the superoxide radical.

Front 10

Noncovalent Bonds

Back 10

Don't depend on the sharing of electron w/ other atoms, but rather on attractive forces b/t atoms having an opposite charge.

Front 11

Ionic Bond

Back 11

Attraction b/t fully charged components

EX. NaCl

Front 12

Hydrogen Bond (H-bonds)

Back 12

When covalently bound hydrogens have a partial (+) charge, due the electronegativity of the other atom, attracts electrons of a second atom. (O,N,&F)

Front 13

Van de Waals forces

Back 13

Attractions b/t nonpolar molecules, are due to transient dipole formation.

Front 14

Acids

Back 14

Release protons

Front 15

Bases

Back 15

Accept protons

Front 16

Amphoteric

Back 16

Molecules can act as either acids or bases

Front 17

pH

Back 17

pH = –log [H+]

Front 18

Biochemicals

Back 18

Carbon-containing molecules produced by living organisms

Front 19

Cholesteral

Back 19

A carbon chain w/ a hydroxly group

Front 20

Functional groups

Back 20

Groups of atoms giving organic molecules different characteristics and properties.

Front 21

What are the four major Macromolecules categories?

Back 21

Proteins

Nucleic acids

Polysaccharides

Lipids

Front 22

Macromolecules

Back 22

Molecules that form the structure and carry out the activities of cells are huge, highly organized

Front 23

What are the two most common linkages b/t functional groups?

Back 23

Ester Bonds

Amide Bonds

Front 24

Ester Bonds

Back 24

Form b/t carboxylic acids and alcohols

Front 25

Amide Bonds

Back 25

Form b/t carboxylic acids and amines

Front 26

Hydroxyl group

Back 26

(—OH)

Front 27

Carboxyl group

Back 27

(—COOH)

Front 28

Sulfhydryl group

Back 28

(—SH)

Front 29

Amino

Back 29

(-NHH)

Front 30

Metabolic Pathway

Back 30

A series of chemical reactions in the cell

Front 31

Metabolic Intermediates

Back 31

The compounds formed along the pathways leading to the end products, might have not functions per se.

Front 32

List the Molecules of Miscellaneous function:

Back 32

Vitamins

Steroid/ A.A. hormones

ATP

Metabolic waste

Front 33

Vitamins

Back 33

Primarily as adjuncts to proteins

Front 34

Carbohydrates

Back 34

Glycans

Front 35

Carbohydrates

Back 35

Simple sugars (monosaccharides) and all larger molecules constructed of sugar Building building.

Functions primarily as stores of chemical energy and building materials.

Front 36

Carbonyl groups

Back 36

(C=O)

Front 37

Glycosidic Bond

Back 37

A bond formed b/t the C1 atom of a sugarl and the hydroxyl group of another sugar. generating an ester linkage (-C-O-C-)

Front 38

Oligosaccharides

Back 38

Small carbohydrate chains.

Front 39

Where are Oligosaccharides found?

Back 39

Bound to cells surface proteins and lipids, and may be used for cell recognition

Front 40

Disaccharides

Back 40

A chain of two carbohydrates.

Front 41

What are disaccharides used for?

Back 41

Sources of readily available energy

Front 42

Polysaccharides

Back 42

are polymers of sugars joined by glycosidic bonds

Front 43

Glycogen

Back 43

is an animal product made of branched glucose polymers

Front 44

Starch

Back 44

is a plant product made of both branched and unbranched and glucose polymers

Front 45

Sucrose

Back 45

Composed of Glucose and Frutose joined by an Alpha (1 → 2) linkage

Front 46

Lactose

Back 46

Composed of Glucose and Galactose Joined by an Beta (1 → 4) linkage

Front 47

What are the Two types of Glycosidic bonds?

Back 47

Alpha (1 → 4) linkage: Type 2

Alpha (1 → 6) linkage: Type 1

Front 48

Starch

Back 48

Is actually a mixture of two different polymers amylose and amylopectin

Front 49

Amylose

Back 49

is an unbranched, helical molecule whose sugars are joined by an Alpha (1 → 4) linkage

Front 50

Amylopectin

Back 50

Is like glycogen but much less branched and have an irregular branch patern

Front 51

Cellulose

Back 51

Unbranched polysaccharides whose sugars are joined by a Beta (1 → 4) linkage

Front 52

Chitin

Back 52

Unbranched polymer of the sugar N-acetylglucosamine. Found in invertebrate exoskeleton.

Front 53

N-Acetylglucosamine

Back 53

Front 54

Glycosaminoglycans (GAG)

Back 54

Polysaccharides is a disaccharide chain(-A-B-A-B-)

Front 55

Triacylglycerol

Back 55

Glycerol molecule linked by ester bonds to three fatty Acids

Front 56

Triacylglycerol

Back 56

Front 57

Fatty Acids

Back 57

Long unbranched hydrocarbon chains w/ a single carboxyl group at one end

Front 58

Lipids

Back 58

A diverse group of nonpolar molecules

Front 59

Steroids

Back 59

Four ringed hydrocarbon skeleton with a hydroxyl group

Front 60

Proteins

Back 60

Are A.A. polymers

Front 61

What are the parts of an A.A.?

Back 61

Alpha Carbon

Amine group

Carboxyl group

Variable R group

Front 62

How are proteins made?

Back 62

By linking together A.A. by peptide bonds into unbranched polypeptide chain

Front 63

Peptide bond

Back 63

The linkage of a carboxyl group to the amino group of one A.A. to the another

Front 64

Polar Charged A.A.

Back 64

The R group contains a relatively strong organic acid or base. As a result they can form ionic bonds.

Front 65

Polar Uncharged A.A.

Back 65

The R group has partial charges and thus can form H-bonds

Front 66

Nonpolar A.A.

Back 66

The R group is hydrophobic and can not form electrostatic bonds. Are found tightly packed w/in the proteins.

Front 67

Glycine

Back 67

Lack of an R group allow for flexibility which allow it to form hinge like regions.

Front 68

Proline

Back 68

Is a hydrophobic, often products kinks or hinges

Front 69

Cystenie

Back 69

Contains a reactive sulfhydryl group, which form a disulfide bond w/ another csytenie in order to stabilize the intricate shape of proteins

Front 70

Disulfide bridge

Back 70

(—S—S—)

Front 71

What are the four levels of protein construction?

Back 71

Primary Structure

Secondary Structure

Tertiary Structure

Quarternary Structure

Front 72

Primary structure

Back 72

The sequence of A.A. in the polymer, is critical to the protein function.

Front 73

Secondary structure

Back 73

The conformation of A.A. into Alpha helix, Beta sheets, hinges, turns, loops, or finger like extensions.

Arrangement of hydrophobic and hydrophilic regions internally or externally

Front 74

Alpha helix

Back 74

the backbone of the polypeptide assumes the form of cylindrical, twisting spiral

Front 75

Tertiary Structure

Back 75

Conformation of the entire polypeptide, a series of noncolavent bonds b/t side chains

Front 76

X-ray crystallography

Back 76

The method use to figure out the Tertiary structure of proteins. By shooting a crystal of the protein with a x-ray the diffracted radiation hits a radiation sensitive plate, where they then use math to discern the structure that could cause the plate pattern.

Front 77

Fibrous proteins

Back 77

elongated shape

Front 78

Globular proteins

Back 78

Compact shape

Front 79

Myoglobin

Back 79

Has a heme prosthetic group that binds O2. The first to globular protein to be discern via X-ray Crystallography

Front 80

Quaternary Structure

Back 80

Refers to proteins and that are composed of subunits

Front 81

Multiprotein complex

Back 81

Different proteins, each w/ a specific function, become physically associated

Front 82

Pyruvate dehydrogenase

Back 82

Convert Pyruvate into Acetyl CoA

Front 83

Molecular Chaperones

Back 83

Helper protein that help unfolded or misfolded proteins achieve the proper folded pattern

Front 84

What are some conditions linked oxygen derived free radicals?

Back 84

Alzheimer, emphysema, cancer, diabetes, rheumatoid arthritis

Front 85

Antioxidants

Back 85

substances that inactivate oxygen derived free radicals. Ex: Glutathione, Selenium, Zinc, beta-carotene, vit. C and E

Front 86

Calorie restriction extends what?

Back 86

Lifespan, b/c there is a decrease in free radical production

Front 87

What modern use if there for chitin?

Back 87

Used to make a strong flexible surgical thread

Front 88

Atherosclerosis

Back 88

Plaque deposits

Front 89

Citrullination

Back 89

The conversion of the A.A. arginine in a protein into the A.A. citrulline

Front 90

Peptidylarginine deiminases (PADs)

Back 90

Replace the aldimine group (=NH) w/ a ketone group (=O)

Front 91

What does cirtullineation do?

Back 91

Control the expression of genes

Front 92

Posttranslational Modification (PTMs)

Back 92

Proteins the DNA doesn't code for, but are made via modification to existing A.A.

Front 93

How would one classify Citrilline

Back 93

A PTMs that is apart of the urea cycle

Front 94

What causes Sickle disease?

Back 94

The Valine replacement of Glutamic acid

Front 95

Selenocysteine

Back 95

A.A. found in prokaryotes and most eukaryotes, but is a PTMs

Front 96

Pyrrolysine

Back 96

A.A. found in some Archea and only one bacterium, but is a PTMs

Front 97

Beta pleated sheet

Back 97

Segment of polypeptide side by side; assume folds of pleated conformation

Front 98

How many A.A. are in one complete cylindrical twist of the Alpha helix?

Back 98

3.6

Front 99

Domains

Back 99

Distinct modules, that independently fold. A functional region that catalysis independently and is found in other proteins.

Front 100

Ribonuclease

Back 100

protein that self assemble

Front 101

Hsp 70 family

Back 101

Bind emerging proteins and prevent inappropriate interactions

Front 102

Chaperonins

Back 102

allow large new proteins to assemble w/o interference from other macromolecules

Front 103

What causes Creutzfeld-Jakob Disease by?

Back 103

Miss folded proteins