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BIO 110 > Chapter Three > Flashcards

Chapter Three Flashcards

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Biology 101 flashcards
1
Q

Structural isomers?

A

atoms are joined together differently, but same chemical composition

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2
Q

cis‐trans isomers?

A

different orientation around a double bond

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3
Q

Optical isomers?

A

occur when C atom has four different groups
attached to it
this makes it an asymmetric carbon / mirror image

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4
Q

Macromolecule?

A

polymer containing thousands or more atoms

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5
Q

describe the hydroxyl group

A

polar charged functional group -OH that help water dissolve molecules by forming hydrogen bonds with water often helps condensation reactions do its thing

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6
Q

describe the Carboxyl functional group

A

COOH
charged acidic, because it gives away a H+. Enters into condensation reaction by giving up an OH, and can be important in energy releasing reactions and is soluble in water

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7
Q

Describe the Amino group

A

NH2
charged basic because it accepts H+ and forms NH3* and enters into condensation by giving up H+ Water soluble and is considered a weak base

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8
Q

describe phosphate group

A

PO4
charged, acidic, because it gives up a H+ water soluble, and important in energy transfer
enters into condensation reaction by giving up OH when bonded to another phosphate

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9
Q

What are the four macromolecules?

A

Proteins
Carbohydrates
Lipids
Nucleic Acids

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10
Q

What are the building blocks of macromolecules?

A

All except lipids have MONOMERS that create polymers

and macromolecules are polymers that have thousands of atoms

building blocks of macromolecules are monomers

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11
Q

What is a polypeptide chain?

A

single, continuous chain of protein monomers, amino acids joined by covalent bonds

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12
Q

Describe the structure of an amino acid.

A

Central carbon with an amino group on one side, carboxyl group on the other

R group (side chain) (variable part) on top, and a hydrogen below the Carbon

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13
Q

How do you group amino acids?

A

side chains (R-groups)
they have certain properties that place them in their groups
There are 20 different amino acids

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14
Q

What is primary structure?

A

the basic sequence (chain) of amino acids (monomers)
this determines the other structures
composed of covalent bonds

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15
Q

what is secondary structure?

A

repeated spacial patterns in different regions of a poly peptide chain that is composed of H bonds

coils and sheets of the primary structure

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16
Q

What are the two types of secondary structure?

A

Alpha helix- right handed coil that results from H bonding between (N-H) and (C=O)

Beta pleated sheets- when two or more chains align and H-bonds form between (N-H) and (C=O)

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17
Q

what is tertiary structure

A

the folding that results in the 3D shape of one polypeptide

it is determined by interactions between R groups, which form disulfide bonds, hydrogen bonds etc.

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18
Q

what is quaternary structure?

A

the overall protein shape due to the interactions of multiple polypeptides chains that make up the protein

19
Q

What is a denatured protein?

A

a protein that’s secondary and tertiary structure and quaternary structure has broken down

20
Q

Why is a proteins primary sequence not broken down during denaturation?

A

because primary structure is made of peptide bonds which are covalently bonded which is very difficult to break

21
Q

What is the process that breaks down primary structure?

A

hydrolysis (adding water breaks the covalently bonded monomers up)

22
Q

What affects secondary and tertiary denaturation?

A

High temperature, pH changes, high concentrations of polar molecules, and non polar substances

23
Q

How do proteins interact with other molecules?

A

They bind non-covalently with specific molecules.

Whether or not a protein can bind with another molecule depends on the
1. shape
2. chemistry of its side chains

If it successfully bonds, it can change the proteins shape

24
Q

state general formula of a carbohydrate

A

(C1H2O1)n

25
Q

why are carbohydrates so important to life?

A
  1. they act as sources of stored energy
  2. they act as transporters of energy
  3. they act as carbon skeletons for other molecules
  4. they form extracellular structures (cell wall)
26
Q

Monosaccharides?

A

simplest sugars
Eg. glyceraldehyde-3C, Ribose-deoxyribose-5C, Glucose, Mannose, Fructose-6C

Can be in straight chain or ring form

27
Q

Disaccharides?

A

two simple sugars linked by covalent bonds
Eg. sucrose, or Lactose
Sucrose = glucose + fructose
Lactose = glucose + galactose

28
Q

Oligosaccharides?

A

3-20 monosaccharides oligo meaning (a few)

Eg. human breast milk

29
Q

Polysaccharides?

A

hundreds or thousands of monosaccharides

Eg. cellulose, starch glycogen

30
Q

What is the bond that joins monosaccharides?

A

glycosidic linkage which is a covalent bond through a condensation reaction

31
Q

What disaccharide is created by linking two beta D glucose by 1st C and 4th C?

A

Cellobiose is formed by glycosidic linkage.

32
Q

Three types of polysaccharides?

A

Cellulose - very stable good for structural component unbranched (tightly packed, linearly

Starch - glucose storage in plants branched (limits the amount of h-bonds that can form, less compact

Glycogen - glucose storage in animals highly branched makes it more compact than starch

33
Q

What are lipids?
What keeps them together?

A

nonpolar hydrocarbons that are insoluble in water

*weak vanderwaals forces are what keep it together

34
Q

why do lipids not have monomers?

A

because the molecules of lipids hydrocarbons don’t bond covalently

molecules of lipids are not glycerol, fatty acids and phosphate, they are simply the C’s H’s

35
Q

Explain the types of lipids

A
  1. fatty acids - non polar hydrocarbon chain with a polar carboxyl group
  2. triglycerides - are three fatty acids plus a glycerol
  3. phospholipids - are fatty acids bound to a glycerol but a phosphate group replaces one fatty acid
36
Q

how are glycerol and fatty acids joined?

A

When the carboxyl of the fatty acids and hydroxyl of glycerol in an ester linkage which is a covalent bond and it releases three water molecules

37
Q

How are triglycerides broken down?

A

Hydrolysis of triglycerides happen when three molecules of water are added

38
Q

Saturated fatty acid and unsaturated fatty acids.

A

Saturated fatty acids are when there are no double bonds between carbons
saturated with hydrogen atoms, tightly packed
usually appear as solids at room temp

Unsaturated fatty acids are when one or more double bonds appear in a hydrocarbon chain, *the double bond kinks prevent close packing
usually appear as liquids at room temp

39
Q

Molecules bearing both polar and non-polar groups are said to be?

A

amphipathic

40
Q

What is the point of lipids?

A
  1. they provide nutrients for organisms

2.store carbon and energy

  1. play structural roles in membranes
  2. function as hormones
  3. thermal insualtion
41
Q

what is a chaperone and why are they important?

A

Chaperone proteins, or molecular chaperones, are proteins that assist others to fold properly during or after synthesis or to refold after partial denaturation

If a protein becomes denatured, the chaperone proteins are useful

42
Q

what are organic compounds made of?

A

They are made of monomers except lipids and the elements that make them up are Carbon, Hydrogen, Nitrogen, and and Oxygen

43
Q

what are the function/ importance of proteins?

A

THEY DO MOST OF THE WORK!
1. Enzymes proteins - they catalyze/speed up reactions
2. structural - provide physical stability and movement
3. defensive proteins -recognize and respond to non self substances
4. signaling proteins - control physiological process (hormones)
5. receptor proteins - receive and respond to chemical signals
6. membrane transporters - regulate the membrane
7. storage proteins - store amino acids
8. transport proteins - bind and carry substances in the cell
9. gene regulation - determine the rate of expression of a gene
10. motor proteins - cause movement of structures in the cell

BIO 110 (19 decks)

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