Biochemistry Lecture

Front 1

Hydrolysis

Back 1

Cleavage of covalent bond by water; Brekdown of bonds

Front 2

Lactate Dehydrogenase

Back 2

Most widely distributed enzymes in the body

Front 3

Hydrocarbons

Back 3

Simplest type of organic molecules; Are C and H containing molecules that are hydrophobic

Front 4

Amino Acid

Back 4

Polymer: Protein

Function: Catalysis, structural elements, energy source

Front 5

Sugars

Back 5

Polymer: CarbohydratesFunctions: Energy source, structural elements

Front 6

Fatty Acid

Back 6

Polymer: Lipids

Functions: Energy source, structural elements of complex lipid molecules

Front 7

Nucleotides

Back 7

Polymer: DNA and RNA

Functions: Genetic information, protein synthesis

Front 8

Amino Acid

Back 8

Biomolecule that contain an amino group and carboxy group

Front 9

Sugar/Carbohydrates

Back 9

Biomolecules that contain both alcohol and carbonyl function groups; Described in terms of both carbon number and type of carbonyl

Front 10

Fatty Acid

Back 10

Monocarboxylic acid that contain an even number

Front 11

Saturated

Back 11

Fatty acid that has no double bond

Front 12

Unsaturated

Back 12

Fatty acid that have double bond

Front 13

Polyunsaturated

Back 13

Fatty Acid that have more than 2 bonds

Front 14

Hydroxyl

Back 14

Properties: Polar

Front 15

Methyl

Back 15

Properties: Nonpolar

Front 16

Carbonyl

Back 16

Properties: Polar

Front 17

Carboxyl

Back 17

Properties: Charged, ionizes to release H+ since carboxyl groups can release H+ ions into solution, they are considered acidic

Front 18

Amino

Back 18

Properties: Charged, accepts H+ to form NH3+. Since amino groups can remove H+ from solution, they are considered basic

Front 19

Phosphate

Back 19

Properties: Charged, ionizes to release H+. Since phosphate groups can release H+ ions into solution, they are considered acidic

Front 20

1. Stable environment

2. Greater complexity in form nd function

3. Exploit environment resources

Back 20

Advantages of multicellular organisms over unicellular

Front 21

1. Complex and Dynamic

2. Organized and Self-sustainable/Self-sustaining

3. Cellular

4. Information base

5. Adapts and Evolves

Back 21

What is Life?

Front 22

Viruses

Back 22

Biologically inert; Composed of DNA or RNA

Front 23

Bacteriophages

Back 23

Reproduce themselves by inserting their genetic information into susceptible host cells

Front 24

Water

Back 24

Predominant chemical component of living organisms; Able to solvate organic and inorganic molecules; excellent nucleophile

Front 25

• Hypothalamic mechanism that control

• ADH

• H2O retention or excretion by tbe kidney

• Evaporative loss

Back 25

Water Regulation dependent on:

Front 26

Water/H2O

Back 26

Has a slight tendency to dissociate into hydroxise ions and protons

Front 27

Bicarbonate and Buffer

Back 27

Maintain pH and ECF between 7.35 and 7.45

Front 28

• pH of arterial blood

• CO2 content of venous blood

Back 28

Acid-Base balance disturbances verified through:

Front 29

Alcohol; Hydroxyl

Back 29

Family; Group Name

Front 30

Aldehyde; Carbonyl

Back 30

Family; Group Name

Front 31

Ketone; Carbonyl

Back 31

Family; Group Name

Front 32

Amines; Amino

Back 32

Family; Group Name

Front 33

Amides; Amido

Back 33

Family; Group Name

Front 34

Thiols; Sulfhydryl

Back 34

Family; Group Name

Front 35

Esters; Ester

Back 35

Family; Group Name

Front 36

Phenylalanine

Valine

Tryptophan

Threonine

Isoleucine

Methionine

Histidine

Arginine

Lysine

Leucine

Back 36

Essential Amino Acid

Front 37

Leucine

Isoleucine

Valine

Back 37

Branched-Chain Amino Acid

Front 38

Histidine

Arginine

Lysine

Back 38

Basic Amino Acid

Front 39

Enzyme

Back 39

Catatyze chemical reactions of all living organism

Front 40

Metabolism

Back 40

The reaction in a living organism

Front 41

Metabolism

Back 41

Acquisition and utilization of energy; Synthesis of molecules needed for cell structure and functioning; Removal of wastes products

Front 42

Nucleophilic Substitution

Elimination

Addition

Isomerization

Oxidation-Reduction

Hydrolysis

Back 42

Biochemical Reaction

Front 43

Nucleophile

Back 43

The element rich species that will react with an electron poor species

Front 44

Substitution

Back 44

Implies that one group replaces another

Front 45

Electrophile

Back 45

Atoms or group that are transferred from the nucleophile to another

Front 46

Elimination

Back 46

A double bond is formed with two atoms in a molecule are removed

Front 47

Addition

Back 47

Two molecules combine to form a single product

Front 48

Hydration

Back 48

The most common addition reaction

Front 49

Isomerization

Back 49

Involves intramolecular shift of atoms of groups

Front 50

Oxidation-Reduction

Back 50

Also known as redox reaction

Front 51

Oxidation-Reaction

Back 51

Occurs when there is a transfer of electrons from a donor to a electron acceptor

Front 52

Oxidizing Agent

Back 52

Electron acceptor

Front 53

Reducing Agent

Back 53

Electron Donor

Front 54

Oxidized Agent

Back 54

When reducing agent donate they become?

Front 55

Reduced Agent

Back 55

When oxidizing agent accept electrons they become?

Front 56

Oxidation

Back 56

Occurs if a molecules gains oxygen or loss hydrogen

Front 57

Reduction

Back 57

Occurs if a molecules loss oxygen or gains hydrogen

Front 58

Tetrahedral Geometry of H2O

Back 58

It is the irregular slightly skewed tetrahedron with O2 at its center; Two H+ and unshared electrons of the remaining two sp3 hybridized orbitals occupy the corners

Front 59

104.5°

Back 59

Degree of bandage of tetrahedral geometry of H2O

Front 60

Ionic/Polar molecules

Back 60

Dissolves readily

Front 61

Non-polar

Back 61

Dissolves poorly

Front 62

Hydrophilic

Back 62

Interact well with H2O and dissolves; It is polar; Soluble

Front 63

Hydrophobic

Back 63

Do not dissolves in water; It is non-polar; Insoluble

Front 64

Amphipathic

Back 64

Both hydrophilic and hydrophobic

Front 65

1. Water molecules form dipole

2. Water molecules form H+ bond

Back 65

Potent Properties of Water

Front 66

1. Increase its dielectric constant

2. Greatly decreass the force of attraction between charged and polar species relative to H2O free environmemt

3. Allows H2O to solvate large quantities of charged compounds

Back 66

Water's strong dipole.....

Front 67

Viscosity

Surface Tension

Back 67

H+ bonding influences the physical properties of H2O including its high?

Front 68

4 H+ bonds

Back 68

How many bonds H2O molecule can form?

Front 69

Hydrogen bonded

Back 69

H2O forms ______ bonded clusters with itself and with other proton donors or acceptors

Front 70

[H+][OH-]

K= -----------------

H2O

Back 70

Ionization of water in formula

Front 71

pH

Back 71

Small concentrations of H+

Front 72

7

Back 72

pOH of water

Front 73

5.55 M

Back 73

M of pure water

Front 74

1.8x10^-16

Back 74

Equilibrium constant of water

Front 75

Acid

Back 75

Has protons tht can dissociate (came off) when dissolved in H2O

Front 76

Base

Back 76

Can absorb protons when dissolved in H2O

Front 77

Increase

Back 77

Addition of base, _____ the pH

Front 78

Decrease

Back 78

Addition of acid, ______ pH

Front 79

Buffers

Back 79

H+ or HO+ added to solution to resist pH changes; Essential to maintain pH

Front 80

Henderson-Hasselbalch Regulation

Back 80

Predicts the response of the H2SO3 system to changes in H+ concentration; Defines the relationship between the pH and the ratio of HCO and H2CO4

Front 81

Ka

Back 81

It is the acid dissociation constant and in a measure of the strength of an acid

Front 82

Stronger

Back 82

The _____ the acid, the more protons will dissociates from it when added to H2O and the larger the value its Ka will have

Front 83

Lower values

Back 83

Large values of Ka translate to lower values of pKa

Front 84

pKa values

Back 84

The lower the _____ of a given acid, the stronger the weak acid is

Front 85

Primary Protein

Back 85

Amount order and sequence of amino acid; Has peptide bond

Front 86

Secondary Protein

Back 86

Alpha helix and beta-pleated sheets; Hydrogen bond

Front 87

Tertiary Protein

Back 87

Structure of protein that are composed of polypeptide bonds

Front 88

Quaternary Protein

Back 88

Structure of protein that have multiple body peptide

Front 89

Sickle Cell Anemia

Back 89

Interchange of valine and glutamic acid

Front 90

COOH-

|

+HN3 ----- alpha ----- H

|

R GROUP

Back 90

Structure of Amino acid

Front 91

• Ampholytes: Contain an amino and carboxyl

• H and -COOH groups bond toalpha carbon are both acidic

• Basic characteristic ia due to the lone pair of electrons of the amino group

• Naturally occuring amino acid belong to the a- configuration

Back 91

Characteristic of Amino Acid

Front 92

Nonpolar

Ala

A

Back 92

Alanine:

Class

3-letter code

1-letter code

Front 93

Polar; Postively Charged Group

Arg

R

Back 93

Arginine:

Class

3-letter code

1-letter code

Front 94

Polar; Neutral Uncharged R Group

Asn

N

Back 94

Aspargine:

Class

3-letter code

1-letter code

Front 95

Acidic Amino Acid

Asp

D

Back 95

Aspartic Acid:

Class

3-letter code

1-letter code

Front 96

Polar; Neutral R charged 4 Groups

Cys

C

Back 96

Cysteine

Class

3-letter code

1-letter code

Front 97

Eukaryotic

Prokaryotic

Back 97

2 Types of Cell

Front 98

Polar; Uncharged

Glu

E

Back 98

Glutamic Acid

Class

3-letter code

1-letter code

Front 99

Polar; Uncharged

Gln

Q

Back 99

Glutamine

Class

3-letter code

1-letter code

Front 100

Nonpolar; Aliphatic

Gly

G

Back 100

Glycine

Class

3-letter code

1-letter code

Front 101

Polar; Positively Charged

His

H

Back 101

Histidine

Class

3-letter code

1-letter code

Front 102

Nonpolar; Aliphatic

Ile

I

Back 102

Isoleucine

Class

3-letter code

1-letter code

Front 103

Nonpolar; Aliphatic

Leu

L

Back 103

Leucine

Class

3-letter code

1-letter code

Front 104

Polar; Positively Charged

Lys

K

Back 104

Lysine

Class

3-letter code

1-letter code

Front 105

Nonpolar; Aliphatic

Met

M

Back 105

Methionine

Class

3-letter code

1-letter code

Front 106

Aromatic

Phe

F

Back 106

Phenylalanine

Class

3-letter code

1-letter code

Front 107

Polar; Uncharged

Pro

P

Back 107

Proline

Class

3-letter code

1-letter code

Front 108

Polar; Uncharged

Ser

S

Back 108

Serine

Class3-letter code1-letter code

Front 109

Polar; Uncharged

Thr

T

Back 109

Threonine

Class

3-letter code

1-letter code

Front 110

Aromatic

Trp

W

Back 110

Tryptophan

Class

3-letter code

1-letter code

Front 111

Aromatic

Tyr

Y

Back 111

Tyrosine

Class

3-letter code

1-letter code

Front 112

Nonpolar; Aliphatic

Val

V

Back 112

Valine

Class

3-letter code

1-letter code

Front 113

Neutral

Back 113

The amino acid is ______ unless there is an extra acid or base on the side chain

Front 114

Neutral Side Chain

Back 114

No side chains

Front 115

L-absolute Configuration

Back 115

A-NH3+ groups are projected to the left

Front 116

D-absolute Configuration

Back 116

A-NH3+ is projected to the left

Front 117

L Configuration

Back 117

Front 118

D Configuration

Back 118

Front 119

Peptide Bond Formation

Back 119

This polymerization is a dehydration reaction

Front 120

Peptide Bond

Back 120

It is rigid and polar; Must have 1 amino terminal and carboxyl terminal

Front 121

Amino Terminal

Back 121

N - terminal

Front 122

Carboxyl Terminal

Back 122

C - terminal

Front 123

Trans Configuration

Back 123

Most stable configuration for the peptide bond with 2 side chains also in trans; Always found in proteins except where they are proline residues

Front 124

Cis Configuration

Back 124

Brings two side chain groups to the same side of the c¢=N bond where unfavorable repulsive steric forces occur between between the two side chain groups

Front 125

Amino Acid Reaction

Back 125

Its is a disulfide bridge reaction

Front 126

Non-essential

Back 126

Human produce _______ amino acids

Front 127

Arginine

Back 127

An amino acid that can make in urea cycle

Front 128

PTT - FYW

Phenylalanine - F

Tyrosine - Y

Tryptophan -W

Back 128

Aromatic AA

Front 129

LAH - KRH

Lysine - K

Arginine - R

Histidine - H

Back 129

Negative AA

Front 130

GAVLIM

Glycine - G

Alanine - A

Valine - V

Leucine - L

Isoleucine - I

Metheonine - M

Back 130

Nonpolar AA

Front 131

SPAGCyTh - SPNQCT

Serine - S

Proline - P

Asparagine- N

Glutamine - Q

Cysteine - C

Threonine - T

Back 131

Polar AA

Front 132

AAA GGG CPST

Alanine

Asparagine

Aspartate

Glutamate

Glutamine

Glycine

Cysteine

Proline

Serine

Tyrosine

Back 132

Non-essential AA

Front 133

PVT TIM HALL

Phenylalanine

Valine

Threonine

Tryptophan

Isoleucine

Metheonine

Histidine

Arginine

Leucine

Lysine

Back 133

Essential AA

Front 134

Arginine

Back 134

Synthesized by mammalian cells but at a rate that is insufficient to meet the growth needs of the body and the majority that is synthesized is cleared to form urea

Front 135

Methionine

Back 135

Required in large amount to produce cysteine if the latter amino acid is not adequately supplied in the diet