Bio Test Chapter 3

Front 1

Structure-function relationship

Back 1

-Functions of macromolecules are directly related to their 3-D shape

-The shape is the result of the sequences and chemical properties of the monomers that make up the polymers

-Relationship between structure and function is an important central theme in biology

Front 2

4 Classes of Macro Molecules

Back 2

Polypeptides, Nucleic Acids, Carbohydrates, Lipids

Front 3

Monomers-Polymer

Back 3

Aminco Acids (20 common)-Polypeptide

Nucleotides (5 Bases)-Nucleic Acid

Front 4

What are Macromolecules

Back 4

Polymers constructed by the formation of covalent bonds between smaller molecules called monomers

Front 5

Amino Acids

Back 5

-All have the same general structure

-H atom

-NH2 Amino group (accept a proton/H+ ion)

-COOH - carboxyl group- donates proton

-R group- variable (side) group

-Charges help amino acids stay in solution, and also influence chemical reactivity

Front 6

Properties of Amino Acids

Back 6

They Vary because the R group Varies

-Nonpolar side chains cannot form H-bonds

-Polar side chains can form H-bonds

Charged side chains can form ionic and H-bonds

Front 7

Most common form of Amino Acids

Back 7

L shape Amino Acids. They are manufactured in cells, and incorporated into proteins.

Front 8

Essential Amino Acids

Back 8

Histidines, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan, Valine

Front 9

Nonessential Amino Acids

Back 9

Alanine, Asparagine, Asparate, Glutamate, Serine

Front 10

Conditionally essential Amino Acids

Back 10

Arginine, Cysteine, Glutamine, Glycine, Proline, Tyrosine

Front 11

Peptide Bonds

Back 11

Covalently link AA's together

-Condensation reaction- combine monomers

-Hydrolysis reactions- break monomers apart

-Residues- term given to AA's that are linked in a chain

Front 12

Polypeptides

Back 12

-The C-N acts like a double bond, so the peptide bond itself cant rotate. The other single bonds can. This makes the molecules flexible

-They are synthesized from the C terminus to the N terminus

Front 13

Four levels of Protein Structure

Back 13

Primary- sequence of Amino acids in a polypeptide

peptide bonds

Secondary- Formation of alpha helices and beta pleated sheets in a polypeptide

Hydrogen bonding between groups

Tertiary- Overall 3D shape of polypeptide.

Quaternary- Shape produced by combination of polypeptides

Front 14

Protein Function Roles

Back 14

-Catalysis of chemical reactions (enzymes)

-Structural support (collagen)

-Molecular transport (hemoglobin)

-Signaling (peptide hormones like insulin)

-Transcription factors- bind to DNA and influence gene expression

Front 15

Factors that influence protein folding

Back 15

-Primary structure

-Chaperones

-Temperature (High temp breaks H bonds and hydrophobic interactions)

-pH

Front 16

Nucleotides

Back 16

Phosphate group, pentose sugar, nitrogenous base

Front 17

Nucleoside

Back 17

Nitrogenous base, pentose sugar

Front 18

phosphodiester bonds

Back 18

covalently link nucleotide monomers

Front 19

Nucleic Acid Primary Structure

Back 19

Order of the nucleotides

Front 20

DNA strands

Back 20

-They have directionality.

-They go from a 3' to a 5' end.

-Nucleotides are added to the 3' end of the chain

-Polymerize in a 5'-3' direction.

Front 21

How is a nonspontaneous reaction made possible?

Back 21

Addition of a phosphate group generates strong repulsive forces raising the potential energy of the substrate molecules

Front 22

ATP

Back 22

Adenosine Triphosphate

-Example of an activated Nucleotide

-Potential Energy stored in activated nucleotides is released when the pyrophosphate is removed

-Energy is released when phosphates are removed by hydrolysis

Front 23

DNA secondary structure- Double Helix

Back 23

-X-ray crystallography measures the distance between atoms by hitting the molecule with X-rays and analyzing how radiation is scattered

-Molecules has a sugar phosphate backbone

Front 24

Chargaff's Rules

Back 24

Purine to Pyrimidines.

A-T

G-C

Front 25

DNA strands

Back 25

They are anti-parallel and they are held together by H-bonding between bases

-Each strand can serve as a template to create a completely new strand

Front 26

DNA function

Back 26

-Information storage molecule in cells

contains genetic information

-DNA is more stable than RNA.

RNA is more reactive due to the -OH instead of the -H at the 2' C.

-DNA is less reactive and more resistant to chemical degradation than RNA

Front 27

DNA vs RNA

Back 27

DNA- information storage, transfer to RNA

RNA- information storage, transfer, assisting in protein synthesis, reaction catalysis

Front 28

Ribozymes

Back 28

Catalytic RNA

Front 29

RNA function

Back 29

-Information storage and transfer (mRNA)

-Reaction catalysis (ribozymes)

-Assisting in protein synthesis (tRNA, rRNA)

Front 30

Monomer-Polymer

Back 30

Amino Acids- Polypeptides

Nucleotides- Nucleic Acids

Monosaccharides- Polysaccharides

Front 31

Carbohydrates

Back 31

Monosaccharide monomers are "simple sugars"

Front 32

4 variations of simple sugars

Back 32

1. placement of the carbonyl group (C=O)

Aldose- CO group at the end of carbon chain

Ketose- CO group in middle of carbon chain

2. Number & arrangement of hydroxyl (-OH) groups

3. Number of C atoms: triose, pentose, hexose

4. linear and alternate ring forms

rare for pentose+ sugars to be linear in an aqueous solution

Front 33

Glycosidic bonds

Back 33

formed between -OH groups and link monomers together.

- occurs when -OH groups on different monosaccharides undergo a condensation reaction

Front 34

Carbohydrates structure and function

Back 34

-Each monomer has at least two Glycosidic bonds

-A 1-4 and B 1-4 bonds are most common

Front 35

Starch

Back 35

-Used for energy storage in plant cells

-mixture of amylose (unbranched) and amylopectin (branched)

Front 36

Glycogen

Back 36

Branches occur every once for every 10 monomers

(unlike starch. once for every 30 monomers)

Front 37

Energy Storage

Back 37

-Plants store sugar as starch, Animals store sugar as glycogen

-Alpha linkages are readily hydrolyzed by certain enzymes

-Starch/Glycogen-> glucose -> ATP

Front 38

Cellulose

Back 38

-used for structural support in cell walls of plants and algae

-3D structure is parallel strands joined together by hydrogen bonds

-monomers linked together by Beta glycosidic bonds and H bonds

Front 39

Cell wall

Back 39

protective sheet occuring outside the cell membrane

Front 40

Chitin

Back 40

-Structural support of the sell wall of fungi and external skeletons of insects and crustaceans.

- has NAG instead of glucose

Front 41

Peptidoglycan

Back 41

-Used for structural support in bacterial cell walls

-has glycosidic bonds between NAG and NAM. cross-linkage is provided by peptide bonds between NAM on different strands

Front 42

Structural Support

Back 42

Beta 1-4 Glycosidic linked strands tend to be insoluble

hard to break down thru hydrolysis

more resistant to degradation and decay

Front 43

Glycoprotein Sugars

Back 43

project outside the cell and have distinctive structures that identify the type or species of cells

Front 44

Lipids

Back 44

Carbon compounds characterized by a physical property (H2O insolubility) instead of a shared chemical structure

-large hydrocarbon component. many C-C and C-H bonds.

Front 45

Major types of Lipids

Back 45

Fats

linked to glycerol. involved in energy storage

Steroids

Polycyclic hydrocarbons with a bulky, for-ring structure; involved in plasma membrane structure and signaling

Phospholipids

hydrophilic head and hydrophobic tail. foundation of the plasma membrane

Front 46

Saturated Vs. Unsaturated

Back 46

The C=C makes the lipid and unsaturated fatty acid.

(not solid at room temp is unsaturated)

Front 47

Fats

Back 47

consist of glycerol linked by ester linkages to three fatty acids

-

Front 48

ester linkage

Back 48

formed when a fatty acid is linked to a glycerol

Front 49

Steroids

Back 49

-characterized by a bulky four ring structure

- Different isoprenoid chains can be attached to hydrophobic rings

-necessary for proper plasma membrane structure.

-crucial in various signaling processes

Front 50

phospholipids

Back 50

consist of two lipid chains linked to glycerol (linked to a phosphate group) <- Linked to a small hydrophilic group

Front 51

amphipathic

Back 51

dual sympathy have both hydrophobic and philic components

Front 52

Phospholipid bilayers

Back 52

-provide plasma membrane structure

-the membrane is selectively permeable.

-small, nonpolar molecules can free flow easily but it is harder for polar molecules and ions.

Front 53

Lipid Bilayers

Back 53

-short and unsaturated is high permeability and fluidity

-Long and saturated makes low permeability and fluidity

Front 54

Factors including plasma membrane permeability

Back 54

Temperature (low temp is bad)

Cholesterol (decreases as cholesterol increases)

Length of hydrocarbon tails- decreases as length of hydrocarbon increases

Saturation of hydrocarbon tails (decreased of degreee saturation increases)

Front 55

Membrane proteins

Back 55

Integral proteins- amphipathic transmembrane proteins that span the bilayer

Peripheral proteins- found on only one side of the membrane and don't pass through it