Biology - Biochemistry I

Front 1

Carbon Formations

Back 1

1. forms covalent bonds, needs 4 electrons per octet rule.
2. Carbon-Carbon & Carbon-Hydrogen are non-polar.
3. Hydrocarbons tend to be poorly soluble.
4. Polar covalent bonds with oxygen or nitrogen are soluble.
5. Stable at different temperatures associated with life.

Front 2

Function Groups

Back 2

Groups of atoms with special chemical features that are functionally important. Exhibits the same properties in all molecules.
ex. Amino, Carboxyl, Methyl, Phosphate

Front 3

Isomers

Back 3

Two Structures with an identical molecular formula but different structures and characteristics.

1. Structural
2. Stereoisomers

Front 4

Structural Isomer

Back 4

contain the atom but in different bonding relationship

Front 5

Stereoisomers Isomer

Back 5

identical bonding relationships, but the spatial positioning of the atoms differs in two isomers.

1. geometric
2. enantiomer

Front 6

Geometric Isomer

Back 6

CIS - if bonds are on the same side
TRANS - if bonds are opposite sides
* both very different chemical properties(stability & sensitivity to head and light)

Front 7

Enantiomer Isomer

Back 7

pair of molecules that are mirrored

1. share identical chemical properties( solubility, melting point)
2. due to orientation of atoms in space, their ability to non covalently bond are different.

Front 8

Polymers

Back 8

Large molecules that formed by linking together many smaller molecules called monomers.

1. Structures depends on
a. structure of monomers
b. number of monomers linked together
c. 3-D way in which monomers are linked

Front 9

Carbohydrates

Back 9

Composed of carbon, hydrogen, and oxygen atoms Cn(H2O)n
1. Sugers

Front 10

Sugars

Back 10

Small carbohydrates that taste sweet.

1. Monosaccharides
2. Disaccharides
3. Polysaccharides

Front 11

Monosaccharides

Back 11

Simplest sugars. Most common are molecules with five carbons, called pentoses, six carbons called hexoses(glucose)

1.

Front 12

Glucose

Back 12

Very water soluble, broken down by enzymes and the energy released is used to make ATP molecules which power many cellular processes. Exists as D & L glucose: mirror images of each other.

Front 13

Disaccharides

Back 13

Two sugars. Carbohydrates composed of two monosaccharides.

1. Bond between two sugar molecules is a glycosidic bond.
2. Hydrolysis of a glycosidic bond in a disaccharide breaks by adding back the water and thus uncouples the two.

Front 14

Polysaccharides

Back 14

when many monosaccharides are linked together to form long polymers.

1. Starch - found in plants, less soluble
2. Glycogen - Present in animal cells and sometimes called animal starch, higher degree of branching contributes to solubility.
3. Cellulose - Polymer of B- glucose, with a linear arrangement of carbon-carbon bonds.
4. Chitin - a tough, structural polysaccharide, forms external skeleton of many insects and the cell walls of fungi.

Front 15

Glycosaminoglycan

Back 15

large polysaccharides that play structural roles in animals

Front 16

Lipids

Back 16

Molecules composed of predominantly of hydrogen and carbon atoms. Non-polar and therefore very insoluble in water. 40% of organic matter in human body.

1. Fats
2. Phospholipids
3. Steroids
4. Waxes

Front 17

Fats

Back 17

Mixture of triglycerides. Formed by glycerol to three fatty acids. A fatty acid chain is made up of carbon and hydrogen atoms with a carboxyl group at the end.

1. Saturated
2. Unsaturated

Front 18

Ester Bonds

Back 18

Each of the three hydroxyl groups in glycerol is linked to the carboxyl group of a fatty acid by the removal of a molecule of water by dehydration reaction.

Front 19

Synthesis of Fatty Acids

Back 19

synthesized by linking together two-carbon fragments

Front 20

Saturated Fatty Acids

Back 20

When all carbons in a fatty acids are linked by single covalent bonds. High melting point, solid at room temperature.

Front 21

Unsaturated Fatty Acids

Back 21

One or more C=C double bonds. Low melting points, liquid at room temperature.

1. Monosaturated Fats - One C=C bond
2. Polyunsaturated Fats - Two or more C=C bonds

Front 22

Fatty acids and Energy

Back 22

Can be metabolized to provide energy to make ATP.

Front 23

Phospholipids

Back 23

similar in structure to triglycerides except the third hydroxyl group of glycerol is linked to a phosphate group instead of a fatty acid.

1. Small polar or charged nitrogen-containing molecule is attached to phosphate. Constitutes a polar hydrophilic region.
2. Fatty acid chain provides a non-polar hydrophobic at the opposite end.
3. In water, when phospholipids become organized into bilayers, their non-polar ends face each other while the polar ends are attracted to water molecules.

Front 24

Steroids

Back 24

Have a distinctly different chemical structure from that of other types of lipid molecules. Four fused rings of carbon atoms form the skeleton of steroids.

1. Estrogen differs from testosterone by having one less methyl group, a hydroxyl group instead of a kelone group, and additional double bonds in one of its rings.

Front 25

Proteins

Back 25

composed of amino acids.

Front 26

Amino Acids

Back 26

Contain carbon, hydrogen, oxygen, nitrogen, and small amounts of other elements. The building blocks of protein.

Front 27

Amino Acid Structure

Back 27

a α-carbon is linked to an amino group and a carboxyl group. The α-carbon also is linked to a hydrogen atom and a side chain.

Front 28

Amino Acid Solubility

Back 28

When dissolved in water, the amino acid group accepts a hydrogen ion and is negatively charged.

Front 29

Side-Chain

Back 29

Their structures are critical features of protein function. The arrangement and chemical features cause proteins to fold and adopt the 3-D shapes.

Front 30

Amino Acid Dehydration

Back 30

Joined together by linking the carboxyl group of one amino acid to the amino group of another, a molecule of water is formed each time two amino acids are joined by dehydration reaction.

Front 31

Peptide Bond

Back 31

The covalent bond formed between carboxyl and amino acid group.

Front 32

Polypeptide Bond

Back 32

The resulting molecule when many amino acids are joined by peptide bonds.

1. Refers to structural unit composed of amino acids. In contrast, a protein is a function unit composed of one or more polypeptides that have been folded and twisted into precise 3-D shapes that carry out a particular function.

Front 33

Hierarchy Structure of Proteins

Back 33

Levels of structure that are dependent of each other. If one level changes, the others change as well.

1. Primary Structure
2. Secondary Structure
3. Tertiary Structure
4. Quaternary Structure

Front 34

Primary Structure

Back 34

its amino acid sequence, from beginning to end determined by genes.

Front 35

Secondary Structures

Back 35

Amino acid sequence folded into a more compact structure.

1. α helix - Polypeptide backbone forms a repeating helical structure that is stabilized by hydrogen bonds.
2. β Sheet - Regions of the polypeptide backbone come to lie parallel to each other.
3. Random Coiled Regions - Some regions along a polypeptide chain do not assume a secondary structure, but are very specific and important to the function of a protein.

Front 36

Teriteary Structure

Back 36

As the secondary structure becomes established due to the particular primary structure, a polypeptide folds and refolds upon itself to assume a complex 3-D shape

Front 37

Quaternary Structure

Back 37

When proteins consist of one or more than one polypeptide chain.

Front 38

Factors that influence Protein Structure

Back 38

1. Hydrogen Bonds
2. Ionic Bonds & Polar Attractions
3. Hydrophobic Effect
4. Van der Waals forces
5. Disulfide Bridges

Front 39

Hydrogen Bonds

Back 39

The large number of hydrogen bonds within a polypeptide and between polypeptides adds up to a strong force that promotes protein folding and stability.

Front 40

Ionic Bonds & Polar Attractions

Back 40

Some amino acid chains are positively charged while others are negatively charged.

1. Positively Charged- May bond to negatively charged side chains via ionic bonds.
2. Uncharged - may interact with ionic amino acids.

Front 41

Hydrophobic Effect

Back 41

Likely to be found in the center of the protein to avoid contact with water.

Front 42

Van Der Walls Forces

Back 42

Atoms within molecules have weak attractions for each other if they are optimal distance apart

Front 43

Disulfide Bridges

Back 43

The side chain of the amino acid cysteine contains a sulfhydroxyl group which can react with a sulfhydroxyl in another cyseine side chain to produce a disulfide bridge or bind which links the two amino acid chains together.

Front 44

Nucleic Acids

Back 44

Account for only 2% of weight in animals. Responsible for storage, expression, and transmission of genetic information.

1. DNA
2. RNA

Front 45

DNA

Back 45

Store genetic information coded for the sequence of their monomer building blocks.

1. Nucleotides
2. Bases

Front 46

Peptide Bond

Back 46

The covalent bond formed between carboxyl and amino acid group.

Front 47

Polypeptide Bond

Back 47

The resulting molecule when many amino acids are joined by peptide bonds.

1. Refers to structural unit composed of amino acids. In contrast, a protein is a function unit composed of one or more polypeptides that have been folded and twisted into precise 3-D shapes that carry out a particular function.

Front 48

Hierarchy Structure of Proteins

Back 48

Levels of structure that are dependent of each other. If one level changes, the others change as well.

1. Primary Structure
2. Secondary Structure
3. Tertiary Structure
4. Quaternary Structure

Front 49

Primary Structure

Back 49

its amino acid sequence, from beginning to end determined by genes.

Front 50

Secondary Structures

Back 50

Amino acid sequence folded into a more compact structure.

1. α helix - Polypeptide backbone forms a repeating helical structure that is stabilized by hydrogen bonds.
2. β Sheet - Regions of the polypeptide backbone come to lie parallel to each other.
3. Random Coiled Regions - Some regions along a polypeptide chain do not assume a secondary structure, but are very specific and important to the function of a protein.

Front 51

Teriteary Structure

Back 51

As the secondary structure becomes established due to the particular primary structure, a polypeptide folds and refolds upon itself to assume a complex 3-D shape

Front 52

Quaternary Structure

Back 52

When proteins consist of one or more than one polypeptide chain.

Front 53

Factors that influence Protein Structure

Back 53

1. Hydrogen Bonds
2. Ionic Bonds & Polar Attractions
3. Hydrophobic Effect
4. Van der Waals forces
5. Disulfide Bridges

Front 54

Hydrogen Bonds

Back 54

The large number of hydrogen bonds within a polypeptide and between polypeptides adds up to a strong force that promotes protein folding and stability.

Front 55

Ionic Bonds & Polar Attractions

Back 55

Some amino acid chains are positively charged while others are negatively charged.

1. Positively Charged- May bond to negatively charged side chains via ionic bonds.
2. Uncharged - may interact with ionic amino acids.

Front 56

Hydrophobic Effect

Back 56

Likely to be found in the center of the protein to avoid contact with water.

Front 57

Van Der Walls Forces

Back 57

Atoms within molecules have weak attractions for each other if they are optimal distance apart

Front 58

Disulfide Bridges

Back 58

The side chain of the amino acid cysteine contains a sulfhydroxyl group which can react with a sulfhydroxyl in another cyseine side chain to produce a disulfide bridge or bind which links the two amino acid chains together.

Front 59

Nucleic Acids

Back 59

Account for only 2% of weight in animals. Responsible for storage, expression, and transmission of genetic information.

1. DNA
2. RNA

Front 60

DNA

Back 60

Store genetic information coded for the sequence of their monomer building blocks.

1. Nucleotides
2. Bases

Front 61

Nucleotide

Back 61

Made up of phosphate group, five carbon sugar, and a single or double ring of carbon and nitrogen.

Front 62

Base

Back 62

1. Purine - double fused rings of nitrogen and carbon atoms. Adenine(A), Guanine(G)
2. Pyrimidine - Single ring of nitrogen and carbon atoms. Cytosine(C), Thymine(T)

Front 63

Helix

Back 63

Two strands are held together by hydrogen bonds between a purine base in one strand and a pyramidal base in the opposite strand. (A-T, G-C) pairing.

Front 64

RNA

Back 64

Involved in decoding this information into instructions for linking together a specific sequence of amino acids to form a polypeptide chain. Consists of a single strand of nucleotides. The sugar is ribose. Contains uracil as pyrimidine base.