Mmg Macromolecules

Front 1

Briefly recap covalent bonding

Back 1

-sharing of a pair of electrons
-strongest bond
-requires energy (releases it when broken; needs enzymes)
-can be polar or nonpolar

Front 2

What is the definition of electronegativity?

Back 2

-attraction of atom for electrons; the more electronegative, the greater the pull its nucleus exerts on electrons

Front 3

What are nonpolar covalent bonds?

Back 3

-atoms with similar electronegativities; electrons are equally shared

Front 4

What are polar covalent bonds?

Back 4

-unequal sharing of electrons due to dignificantly different electronegativities

Front 5

What are ionic bonds?

Back 5

-electrons donated/accepted to give full charges and outer shells
-important in osmotic changes
-easily broken in water and reforming the ions again

Front 6

What are Hydrogen bonds?

Back 6

-electrical attraction between partially charge H and full or partial neg charge on another (or same) molecule
-weakest of bonds
-hold DNA strands together
-in protein molecules, responsible for 2, 3, and quaternary structures

Front 7

What are macromolecules made up of? And what makes these up?

Back 7

-polymers
-monomers

Front 8

What are some examples of macromolecues?

Back 8

-lipids
-carbohydrates
-proteins
-nucleic acids

Front 9

What are lipids known as and what are they composed of?

Back 9

-triglycerides
-fatty acids bonded to C3 (tertiary carbon) alcohol glycerol
-saturated means no c=c
-unsaturated means one or more c=c

Front 10

What does amphipathic mean?

Back 10

-hydrophilic and phobic
-important for cellular membranes

Front 11

Describe Steroids (make-up and use).

Back 11

-consist of four rings (5 or 6 C's) fused together and used as hormones in mammalian cells (testosterone, estradiol, progesterone)

Front 12

Describe Sterols (make-up only)

Back 12

-basically, steroids with an -OH functional group
-found in eukaryotic membranes
-rigid, planar molecules that provide rigidity to membranes

Front 13

What is ergosterol?

Back 13

-a sterol found in fungal membranes; target of many anti-fungal drugs

Front 14

What are 6 functions of polysaccharides?

Back 14

-long-term storage of chemical energy
-readily available energy source
-part of backbones of nucleic acids
-converted to amino acids
-form cell wall
-involved in intracellular interactions between animal cells

Front 15

What are polysaccharides sometimes coupled with?

Back 15

-with proteins= glycoproteins
-with lipids= glycolipids

Front 16

What is responsible for forming the bonds in macromolecules?

Back 16

-enzymes

Front 17

What do starch, glycogen, and cellulose have in common?

Back 17

-all composed of glucose

Front 18

What does the stereochemistry of bonds determine in polysaccharides?

Back 18

-whether poly-glucose becomes starch, glycogen or cellulose

Front 19

What elements make up polypeptides and proteins?

Back 19

-structure
-enzymatic catalysis
-regulation
-transportation

Front 20

What functional groups make up amino acids?
What affects molecule interaction?

Back 20

-amino group
-carboxyl group
-functional R group
*R groups affect how amino acids interact with one another and how protein interacts with other molecules

Front 21

What are the 21 common amino acids?

Back 21

-glycine -alanine
-valine -leucine
-isoleucine -serine
-threonine -aspartate
-asparagine -glutamate
-glutamine -cysteine
-selenocysteine -tyrosine
-methionine -phenylalanine
-tryptophan -lysine
-arginine -histidine
-proline

Front 22

What are the two forms amino acids and sugars can exist in?

Back 22

-optical isomers
-enantiomers
*same chemical formula

Front 23

What forms are synthesized and utilized amino acids in?
How about sugars?

Back 23

-L form
-D form
*enzymes must be able to discriminate one form from another

Front 24

How are peptide bonds formed?

Back 24

-amino acids are polymerized into a polypeptide through the loss of a water molecule (dehydration)

Front 25

What are the four structures of polypeptides and how are they held together?

Back 25

-primary; peptide bonds
-secondary; folding and then held with H-bonds
-tertiary; folding and held with H-bonds, covalent S-S bond between cysteine AA, and interactions between R groups
-quaternary; interactions between 2 or more polypeptides and the same as 3' (no cysteine?)

Front 26

What are the two structures of secondary structures?
Which one is strongest/rigid?

Back 26

-alpha-helix structure (more flexible)
-beta-sheet structure (more rigid)

Front 27

What can cause a protein to denature?

Back 27

-extreme pH
-high temperature
-chemicals
-metals

Front 28

What does denaturing do to proteins?

Back 28

-causes loss of protein function by affecting sexondary, tertiary, and quaternary structures (NOT primary structure) of protein
*depending on harshness of denaturation, proteins can renature

Front 29

What is so important about denaturing proteins since it is normally thought of as bad?

Back 29

-important in destroying microbes

Front 30

What and where are nucleic acids?

Back 30

-information carriers of the cell
-found as polynucleotides of either DNA or RNA

Front 31

What are nucleotids composed of?

Back 31

-sugars, nitrogen bases, and phosphates

Front 32

Besides DNA/RNA, what are nucleotides important for?

Back 32

-important energy sources
-metabolic regulatory molecules

Front 33

In DNA, does it exist as a single or double strand?
-How is it held together?

Back 33

-double
-base pairing between purines and pyrimidines by H-bonding hold it together
*A with T and G with C

Front 34

RNA is single stranded, but was can lead to a secondary RNA structure?

Back 34

-intrastrand base pairing
(A with U, G with C)

Front 35

What does A, T, G, C, U stand for?

Back 35

-adenine
-thymine
-guanine
-cystine
-uracil