Bio Examkrackers Ch 1

Front 1

Hydrophilic molecules

Back 1

Dissolve easily in water because their (-) charged ends attract the (+) charged ends of H+ and their (+) charged ends attract the - oxygen

Front 2

water

Back 2

-Universal solvent used for chemical rxns
-70-80% of cell mass
-small polar molecule
-hydrogen bonds keep it liquid at typical cell temp

Front 3

Hydrogen bonds

Back 3

-provide strong cohesive forces between water molecules
-these cohesive forces squeeze hydrophobic molecules away from water and cause them to aggregate
-VERY strong bonds

Front 4

hydrolysis

Back 4

-most macromolecules are broken apart by hydrolysis
-most common catabolic rxn in humans

Front 5

Dehydration synthesis

Back 5

-Most macromolecules are formed by dehydration
-Water is a byproduct

Front 6

Lipids

Back 6

-biological molecule with low soulubility in water
-high solubility in non-polar organic solvents
-hydrophobic

Front 7

Seven Major Lipid Groups

Back 7

1. Fatty acids
2. Triacylgylercols
3. Phospholipids
4. Glycolipids
5. Steroids
6. Terpenes
7.Waxes

Front 8

Functions of Lipids

Back 8

1. Long Term Energy Storage

2. Cellular Organization/Structure

4. Signaling Molecules: Can pass through cell membranes

5. Precursor for Vitamins and Hormones

Front 9

Function of Glycolipids

Back 9

1. Cellular Recognition

2. Provides Energy

Front 10

Sphingolipids

Back 10

-Contain amino alcohol backone instead of a glycerol backbone

-Found in cell membrane

Front 11

Carboxylic Acid

Back 11

COOH
carbon with a oxygen and OH

Front 12

Fatty Acids

Back 12

-building blocks for most complex lipids
-long chain of carbon with carboxylic acid end
-max of 24 carbons
-saturated or unstaturated
-Composed of long carbon chains with a carboxylicacid at one end.

Front 13

Saturated Fatty Acid

Back 13

single carbon bonds ONLY

Front 14

Unsaturated Fatty Acids

Back 14

one or more double carbon bonds

Front 15

Oxidation of Fatty acid

Back 15

-Enables large amounts of chemical energy to be used in a cell

Front 16

Function of Fatty Acids

Back 16

LONG TERM ENERGY STORAGE (Due to massive # of C-H bonds)

Front 17

Triacylglycerols

Back 17

-Triglycerides or fats/oils

-3 carbon backbone (glycerol) attached to 3 fatty acid chains

Function:
-Metabolic Energy Storage,
-Thermal insulation/padding

Front 18

Adipocytes

Back 18

-fat cells
-specialized cells whose cytoplasm contain almost all trigylcerides

Front 19

Phospholipids

Back 19

-3 carbon glycerol backbone
-polar phosphate group replaces one fatty acid at opposite end, making phosphate end polar and fatty acid end nonpolar
**Amphipathic, good for memebranes

Front 20

Amphipathic

Back 20

Polar and Nonpolar

Front 21

Glycolipids

Back 21

-Similar to Phosphoglycerides, but one or morecarbohydrates attached to glycerol backbone INSTEAD of phosphategroup. ·

-Amphipathic ·

-Found in nervous system (mylenated cells)

Front 22

Steroids

Back 22

-Function: Regulate Metabolic activities
-4 ringed structure
-Includes hormones
-Vitamin D
-Cholesterol (membrane component)

Front 23

Cholesterol is important in..

Back 23

Membranes

Front 24

Lipids are ___________ in aqueous solutions

Back 24

Insoluble

Front 25

Waxes

Back 25

Lipid formed by an ESTER linkage between a longchain alcohol and a long chain fatty acid

Front 26

Function of Phospholipids

Back 26

Structural component of membranes

Front 27

Function of Triacylglycerols

Back 27

-Metabolic energy storage
-provide thermal insulation/padding

Front 28

Terpenes

Back 28

-Pigments in the body

-Vitamin A

Front 29

Function of Steroids

Back 29

-Regulate metabolic activity
-some fatty acids (eicosanoids) serve as hormones

Way to remember: Anabolic Steroids (bodybuilders) causes INCREASE in regulation of metabolic activity . Increase=Bigger muscles.

Front 30

Proteins are made of ______
linnked by ______ bonds

Back 30

amino acids, peptide

Front 31

Proteins =

Back 31

Polypeptides

Front 32

Proteins are made up by _____ amino acids

Back 32

20 alpha amino acids

Front 33

Essential Amino Acids

Back 33

-body cannot make them
-must be digested
-10 in total

Front 34

Amino acids differ in their...

Back 34

side chains (-R group)

Front 35

Proteins are..

Back 35

Polar, nonpolar, acidic, basic

Front 36

Protein Primary Structure

Back 36

Number and sequence of amino acids in a polypeptide

Front 37

Protein single chain (primary structure) can twist into..

Back 37

Seconday structure

Front 38

Alpha-Helix and Beta Pleated Sheets have __________ bonds

Back 38

Hydrogen bonds between the carbonyl oxygen adn teh hydrogen on the amino group

Front 39

Secondary structure of Protein

Back 39

Conformation of protein

Front 40

Tertiary Structure

Back 40

3-D shape when peptide chains curl and fold
-Disulfide bonds btw 2 cysteine amino acids on different parts of the chain

Front 41

Tertiarty structure can be created by

Back 41

1. covalent disulfide bonds
2. ionic (electrostatic) interactions
3. Hydrogen bonds
4. Van Der Waals forces
5. Hydrophobic side chains pushed away from water

Front 42

Quaternary Structure

Back 42

2 or more polypeptide chains bind together

Front 43

Denaturation

Back 43

protien strucutre disrupted, loses seconday, tertiary, and quaternary
When denaturing agent removed protein can return to original

Front 44

Globular Proteins

Back 44

enzymes
hormones
membrane pumps and channels
membrane receptors

Front 45

Denaturing Agents

Back 45

examples:
urea, salt, change in pH, temperature

Front 46

Proteins contain..

Back 46

NITROGEN!

Front 47

Carbohydrate empirical formula

Back 47

sugar, saccharides
CH2O

ex: glucose, hexoses

Front 48

Glycogen

Back 48

-in all animal cells
-lots in muscle and liver cells
-liver regulates blood glucose levels

Front 49

Glucose alpha, beta linkage breakdown

Back 49

Animals eat alpha linkages

Only bacteria can breakdown beta linkages

Front 50

Starch

Back 50

Comes from glucose in plants and has 2 forms:
1. amylose
2. amylopectin

Front 51

Cellulose

Back 51

Comes from glucose in plants and has BETA-linkages

Front 52

3 Components of Nucleotides

Back 52

1. Pentose
2. Nitrogenous base
3. Phospate group

Front 53

5 Nitrogenouse Bases

Back 53

1. Adenine
2. Guanine
3.Cytosine
4. Thymine
5. Uracil

Front 54

Nucleotides are joined by..

Back 54

Phosphodiester bonds btw teh phosphate group of one nucleotide and the 3rd (3') carbon of pentos
5' to 3'

Front 55

In DNA, Adenine pairs up with..

Back 55

Thymine, double bond
DNA

Front 56

In DNA, Guanine pairs up with..

Back 56

Cytosine with a triple bond
DNA

Front 57

In RNA, adenine pairs up with..

Back 57

Uracil by a double bond

Front 58

ATP

Back 58

-nucleotide
-source of readily avaliable energy for cells

Front 59

Cyclic AMP

Back 59

-in secondary messenger systems
-nucleotide

Front 60

NADH and FADH2

Back 60

-coenzymes in the Krebs cycle
-nucleotides

Front 61

Minerals

Back 61

-dissolved inorganic ions inside the cell
-create electrochemical gradiaents across a membrane
-assist in transport of substances in and out of cell
-act as cofactors for enzymes

Front 62

Enzymes

Back 62

-globular proteins
-act as a catalyst
-lowers activation energy
-increases the rate of a rxn

Front 63

Substrate

Back 63

-reactants that an enzyme works on
-generally smaller than the enzyme

Front 64

Active site

Back 64

-position on enzyme where the substrate binds by noncovalent bonds
-forms enzyme-substrate complex

Front 65

Enzyme Specificity

Back 65

enzymes are designed to work on specific substrate or groups of closely related substrates
Ex: lock and key theory

Front 66

Induced Fit

Back 66

The shape of bopth teh enzyme and substrate are altered upon binding
This increases specificity and helps the rxn proceed

Front 67

Saturation Kinetics

Back 67

As the relative concentration of the substrate increases, the rate of the rxn increase, but to a lesser degree until a max rate (Vmax) has been achieved

Front 68

V max =

Back 68

Enzyme concentration

Front 69

Optimal Enzyme Temp

Back 69

37 degrees C

Front 70

Cofactors

Back 70

-Non protein that helps an enzyme reach optimal activity

-can be coenzymes or metal ions

Front 71

Coenzymes

Back 71

are cosubstrates and prosthetic groups that bind to enzymes

Front 72

Irreversible Inhibitors

Back 72

Agents which bind COVALENTLY to enzymes and disrupt their function
Ex) penicilin

Front 73

Competitive Inhibitors

Back 73

Compete with the substrate by binding NONCOVALENTLY to the active site

Front 74

Noncompetitive Inhibitors

Back 74

Bind NONCOVALENTLY to an enzyme at a spot OTHER THAN the active sire adn change the enzymes conformation, does not prevent the substrate from binding

Front 75

Enzymes are regulated by..

Back 75

1. Protelytic cleveage
2. reversible covalent modification
3. Control Proteins
4. Alloseteric interactions

Front 76

Zymogen or proenzyme

Back 76

Inactive enzyme

Front 77

Allosteric Interactions

Back 77

The modification of the enzyme configuration resulting from the inhibitor at a specific binding site on the enzyme

Front 78

Negative feedback is the same as...

Back 78

Feedback inhibition

Front 79

Negative Feedback
Feedback Inhibition

Back 79

One product from an enzyme downstream in a rxn comes back and inhibits the enzyme, provides a shutdown mechanism for a series of enzyme rxns when a sufficient amt of product has been reached

Front 80

Positive Feedback

Back 80

When the product returns to activate teh enzyme

Front 81

Allosteric Regulation

Back 81

Feedback inhibitors bind to the enzyme and cause a conformational change, there are allosteric inhibitors and activators

Front 82

Positive Cooperativity

Back 82

The 1st substrate changes the shape of the enzyme allowing other substrates to bind more easily

Front 83

Glycerol

Back 83

A 3-Carbon Backbone