Final Exam Review I

Front 1

Polar covalent bonds

Back 1

One atom is more electronegative than the other

Front 2

Non polar covalent bonds

Back 2

Atoms share equal electrons

Front 3

Hydrogen bonds

Back 3

Weak chemical bonds that must be broken down to vaporize

Front 4

Functional Group- Carboxyl

Back 4

COOH, polar, e.g. organic acid and amino acids

Front 5

Functional Group- Hydroxyl

Back 5

OH, polar, e.g. sugars

Front 6

Functional Group- amino

Back 6

NH2, polar, amino acids

Front 7

Functional group- Sulhydryl

Back 7

SH, polar, cysteine

Front 8

Functional group- Phosphate

Back 8

PO4, polar, ATP and DNA

Front 9

Functional group- methyl

Back 9

CH3, nonpolar, methylated DNA

Front 10

Saturated carbon chains

Back 10

Long hydrocarbon chains (more hydrogen) molecules packed together

Front 11

Unsaturated carbon chains

Back 11

Can not pack closely together, kinks, liquid

Front 12

Organic molecules- proteins

Back 12

enzymes

Front 13

organic molecule- carbohydrates

Back 13

cannot be electrically charged, long hydrocarbons

Front 14

organic molecule-lipids

Back 14

fats, triglyc., Low density

Front 15

organic molecules- Nucleic acid

Back 15

5C sugar, phosphate and a nitrogenous base

Front 16

Macromolecules are synthesized by ?

Back 16

Dehydration reaction

Front 17

Macromolecules are digested by ?

Back 17

Hydrolysis (break down of water)

Front 18

Properties of water

Back 18

Good solvent
Regulates temperature (high specific heat and vaporization)]
Good density (expansion upon freezing)
Cohesive (high surface tension)

Front 19

How do this properties of water help? *

Back 19

When water is it in liquid stage, hydrogen bonds are very fragile therefore bonds can break and form with greater frequency.

Front 20

Acid Base Balance

Back 20

0-6 Acid, More H+
7 Neutral, H+= OH-
8-14 Base, more OH-

Front 21

Hydrophillic

Back 21

affinity for water, love

Front 22

Hydrophobic

Back 22

repel water

Front 23

Primary structure

Back 23

sequence of amino acids

Front 24

Secondary structure

Back 24

polypeptide chain coiled with alpha helix and Beta helix are joined by hydrogen bonds

Front 25

Tertiary Structure

Back 25

Fully dimensional shape of a fully polypeptide

Front 26

Quaternary Structure

Back 26

2 or more polypetide chains

Front 27

Disulfide Bonds

Back 27

Maintain the shape of a polypeptide chain

Front 28

Denaturation

Back 28

Change of the 3 dimensional shape due to disruption, hydrogen bonds, disulfide bridges

Front 29

Endomembrane System

Back 29

Nucleus- Nuclear envelope
Smooth ER (cells that secrete lipids) Rough ER- make and secrete proteins and vesicles ready for the Golgi- modigy the proteins, e.g. insulin. COnverted into lysosomes which fuse for digestion into the plasma membrane

Front 30

Perixosomes

Back 30

break fatty acids and detoxify

Front 31

Chloroplasts

Back 31

Site of photosynthesis, make ATP, @ Calvin cycle

Front 32

Mitichondria

Back 32

Site of cellular respiration, make ATP, @ krebs cycle

Front 33

Simple diffusion

Back 33

movement of any substance from high to low concentration, no protein or energy required

Front 34

Facilitated Diffusion

Back 34

movement of any substance from high to low concentration, no energy, protein required

Front 35

Active transport

Back 35

Movement of any substance against its concentration gradient

Front 36

Endocytosis

Back 36

Plasma membrane surrounds as part of the environment

Front 37

Exocytosis

Back 37

Vesicle fuses with a plasma membrane and its released

Front 38

Endergonic reactions:

Back 38

Absorbs free energy from its surroundings, Final energy is greater than initial, G is positive, Reactions require energy input to ocurr

Front 39

Exergonic reaction

Back 39

Final is less than initial, G is negative, spontaneous, energy is added

Front 40

ATP hydrolisis

Back 40

Exergonic reaction, ATP bonds are broken down, the energy released if for chemical and mechanical work (shape and abulity to bind to a cytoskeleton)

Front 41

Energy coupled reactions

Back 41

They trap all the energy and then they release it from endergonic to exergonic

Front 42

Induced Fit Model

Back 42

Proteins speed up the reaction but are not used in the reaction. Bring chemical groups of the active site in positions that enhance the ability to break down a reaction

Front 43

Shape and Change

Back 43

the enzyme structure shape and change can make it specific to catalyze a reaction

Front 44

Competitive Inhibitor

Back 44

Block substrate from the enzyme competing for an active site

Front 45

Noncompetitive inhibitor

Back 45

CHanges the shape of the enzyme altering the active site

Front 46

Second Law of thermodynamics

Back 46

When reaction occurs entropy increases

Front 47

Total solute gradient:

Back 47

Necessary to cause osmotic movement across a membrane

Front 48

G

Back 48

For two reactions to be energy coupled, their G must equal to 1

Front 49

weak acid into the inner membrane?

Back 49

ATP increases more H concentration more diffusion of protons

Front 50

Proton Pump- how it uses ATP

Back 50

Exergonic ADP + P=ATP
Endergonic: H go down its concentration gradient

Front 51

enzymes speed up ? the reactions.. in terms of energy and physical

Back 51

Energy? they activate the energy
Physical? bind to active site, stress or weaken