Unit 1: Biochem - Macromolecules Flashcards Preview

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Flashcards in Unit 1: Biochem - Macromolecules Deck (56)
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1
Q

6 Functions of proteins

A
Repair/Maintenance
Transportation/Storage
Energy
Hormones
Enzymes
Antibodies
2
Q

Peptide Bond

A
  • Carboxyl group on one reacts with amine group, releasing water molecule
  • Only found between amino acids
3
Q

Primary structure

A

Specific sequence of AA’s, determined by nucleotides

4
Q

Secondary structure

A
  • α helix/β pleated sheet
  • Three dimensional structure of a polypeptide chain -
  • Formed by H bonds between amine group of AA, carboxyl group of other
5
Q

Motifs

A

Recognizable combinations of secondary structure

6
Q

Tertiary Structure

A

Final folded shape of polypeptide, formed by interactions between R groups
Disulfide bridges

7
Q

Disulfide bridges

A
  • Sulfhydryl groups of two cysteine monomers are brought closer together by the folding of the proteins
  • Sulfur of one cysteine bonds to the sulfur of the second
8
Q

Quaternary structure

A
  • Aggregation of two polypeptide subunits
9
Q

Denaturation

A

Unfolds proteins

Breaks s-s bonds, h-bonds, LDF’s, ionic bonds via HYDROLYSIS

10
Q

Chaperonins

A

Folds misfolded proteins using ATP

11
Q

ENVIRONMENTAL causes of denaturation

A

Heat
pH - H+ sticks to R groups messes up charge of amino acid
Salt - Same
Solvent - Non polar solvents screw up hydrophilic/hydrophobic ends

12
Q
Carb Basics
(Function, structure)
A

CH2O

- Short term energy storage (4 kCal/gram)

13
Q

Glycosidic Linkages

A
  • Between two monosaccharides
  • Uses dehydration synthesis
  • α 1-4 linages, α 1-6 linkages
14
Q

Structural Isomers

A

Different atoms connected (most different of isomers)

Glucose-Aldose + Fructose-Keytose

15
Q

Stereoisomers

Geometric/Enantiomers

A

Stereo isomers - Same atoms connected, different shape
Geometric - Have double bonds, or rings
Enantiomers - Mirror Images

16
Q

Chiral Carbon

A

carbon atom that is attached to four different types of atoms or groups of atoms

17
Q

Starch basics

Function, Properties, Structure

A
  • Short term energy storage in plants
  • Polar + Hydrophilic
  • Not soluble because or size
  • instead, amylase hydrolyzes alpha 1-4 bonds in starch
18
Q

Short term energy storage in animals

A

Glycogen

Liver + muscle

19
Q

Cellulose basics

Function, Structure

A
  • Found in plant cell walls and algae
  • Monomer is B glucose (OH above C)
  • Flipping glucose allows for hydrogen bonding between forming lattice
20
Q

Cellulose is broken down by

A

Cellulase - breaks B 1-4 bonds, leaving us with glucose!

21
Q

Fiber

A

Undigested cellulose!

22
Q

Chitin

A
  • Structure in arthropod exoskeletons, fungi, cell walls
  • Monomer - N-acetyl glucosamine
  • B bonds 1-4, H bonds, and others between linear chains
23
Q

Peptidoglycan

A
  • Bacterial/Prokaryote cell walls

- CHN Monomer with cross linked peptide chain attached

24
Q

Lipid Basics

Structure, Properties

A

C, H, O, Sometimes P

- Non-polar, don’t dissolve in water

25
Q

Fats

Functions, structure

A
  • Triacylglycerols/Triglycerides
  • Long term energy storage - 9kcal/g
  • Insulation and cushioning
  • 3 Fatty acids + glycerol through ester linkage
  • Common in animals, some plants (avocados, seeds)
26
Q

Why do fats have so much energy?

A
  • Non-polar bonds are stable, hard to break, release a lot of energy
  • More energy and weigh less than carbs bc of molecular formula
  • Always more H than O, H weighs less 1:16
27
Q

Monomer of a lipid

A

NO MONOMER OF A FAT LIPID

28
Q

Ester linkage

A

Dehydration synthesis to bond glycerol to fatty acid

leaves O and CO

29
Q

Saturated

A

No double bonds, max number of H, STICKS

30
Q

Unsaturated

A

At least one double bond along fatty acid chain, fewer H

31
Q

Fatty Acids

A

12-20 carbons long

3 fatty acids per fat molecule

32
Q

Omega

A

C=C closest to the left

Essential fatty acids - must be consumed cause your body can’t make a bond in that specific place

33
Q

Fats = Fatty acids?

A

NO

fats are larger, more LDF’s hold together better

34
Q

Trans Fats

A
  • People wanted spreadable oils - hydrolyze oils to make solid
  • Trans configuration
35
Q

Hydrolization

A

Addition of hydrogen to make unsat - sat

36
Q

Cis/Trans

A

Cis - Functional group on same sides of carbon chain

Trans - Functional group on opposing sides

37
Q

Phospholipids

A
  • Make up membranes
  • Hydrophobic tail / Hydrophilic Head
  • Head is phosphate group and glycerol
  • One unsaturated fatty acid tail, one saturated
  • Tails connected by ester bonds
38
Q

Amphipathic

A

One part hydrophobic, One hydrophilic

39
Q

Steroids

A
  • 3 Hexagons, one pentagon, made of C + H
  • Non-polar
  • Rigid
  • Each defined by their chemical structure
40
Q

Cholesterol

A
  • Precursor for other steroids

- In plasma membranes for structure

41
Q

Last group of lipids

A

Not fats, phospholipids, or steroids,

Terpane (citronella)

42
Q

Nucleic Acid Basics

Structure, Functions

A

CHONP

  • Monomer: Nuctleotides joined by phosphodiester bonds
  • Catalyze reactions as RNA
  • Energy transfer - ATP
  • Structural purposes
43
Q

Nucleotide

A

Phosphate group, pentose, nitrogenous base

44
Q

Phosphodiester bond

A

Dehydration synthesis between phosphate group and 3 carbon

45
Q

Purines/Pyrimidines

A

Purines - Double ring - Adenin, Guanine

Pyrimidines - Single ring - Cytosine, thymine, Uracil

46
Q

Nitrogenous base bonds

A
A = T/U
C = G
47
Q

Strand 5 VS. 3

A
  • Phosphate group on strand 5
  • Hydroxyl group on strand 3
  • Oxygen always points towards 5
48
Q

RNA

A
  • Ribose, ACGU, single stranded, inconsistent shape
  • Can h bond if in correct shape (TRNA)
    rRNA - Ribosomes
    Ribozymes - Catalyze reactions
    mRNA - Transfer of info
49
Q

DNA

A
  • Deoxyribose, ACGT, double helizz
  • 2 polynucleotide strands, held together by H bonds
  • 3 rings, keeps consistent shape
50
Q

Why is DNA strand antiparallel?

A

A + T have h bonding pairs that fit, but only if one is flipped, thus DNA strands run anti parallel

51
Q

What is always slightly positive in an H bond?

A

H

52
Q

ATP

A
  • Adenosine Triphosphate
  • Nitrogenous base + pentose + 3 phosphate groups
  • ENERGY TRANSFER
  • Bond between phosphate - Phosphoanhydride
53
Q

Nucleoside

A

Nitrogenous base + pentose

54
Q

Why does ATP supply so much energy

A
  • Negative charges on O- repel each other, making molecule unstable, easy to break
  • Releases small amounts of energy, but accessible
55
Q

NAD+

A
  • Nicotinamide Adenine Dinucleotide
  • Because of opposite charge, molecule picks up ATP, goes back and forth depending on surroundings
  • Performs redox reactions
56
Q

Redox reactions

A

Transfers electrons between molecules