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Biochemistry Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Hydroxyl Group

A
  • OH ending

- Alcohols (“-ol”)

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2
Q

Carbonyl Group

A

=O

  • Aldehydes (terminal) “-al”
  • Ketones (non-terminal) “-one”
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3
Q

Carboxyl Group

A
  • COOH
  • Carboxylic acid “-oic acid”
  • terminal
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4
Q

Amino Group

A
  • NH2

- Amines “amine”

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5
Q

Sulfhydryl Group

A
  • SH
  • Thiols (“‘thiol”)
    i. e. ethanethiol
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6
Q

Phosphate Group

A
  • PO4
  • Organic phospate (“phospho-“) prefix
    i. e. phosphopropane
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7
Q

Organic Molecules

A
  • Carbon as primary element

- Usually long and complex

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8
Q

Inorganic Molecule

A
  • Carbon not primary ingredient

- Usually small and simple

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9
Q

Polar Bonds

A

-Atoms have unequal sharing of electrons

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10
Q

Non-polar bonds

A

-2 atoms with same/similar EN

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11
Q

Glycosidic Linkage

A
  • 2+ carb monomers link together in condensation rx to form polysaccharides
    i. e. glucose + glucose -> maltose
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12
Q

Ether Bond

A
  • Condensation b/w two alcoholsbombines

i. e. ethanol +propanol -> ethoxypropane

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13
Q

Ester Bond

A
  • Condensation b/w alcohol and organic acid

i. e. methanol + ethanoic acid -> methylethanoate

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14
Q

Peptide Bond

A

-Condensation rx b/w 2 amino acids

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15
Q

Disulphide Bond

A
  • thiols combine
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16
Q

Phosphodiester Bond

A
  • Phosphate in condensation rx with alcohol group on separate organic molecules
  • Links nucleotide monomers
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17
Q

Carbs

A
  • Short term energy storage
  • All are aldehyde/ ketones
  • “ose” usually
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18
Q

Alpha linkage

A

-Hydroxyl group points down

a+ a = down

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19
Q

Beta linkage

A

-Hydroxyl group points up

beta +beta = up

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20
Q

Polysaccharides

A
  • Contain many units of glucose
    i. e. starch, glycogen, cellulose, chitin
  • branched chain - glycogen, amylopectin
  • straight chain- amylose
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21
Q

Glycogen

A
  • Made of amylose and amylopeptin
  • Energy storage in animals
  • Glucose stored as glycogen when not in use
22
Q

Starch

A
  • Glucose units facing same direction (weaker bonds)
  • Can be digested
  • Soluble
23
Q

Cellulose

A
  • Glucose units facing different direction (stronger bonds- good for building)
  • Can’t be digested
  • Insoluble
24
Q

Insulin

A

-lowers blood sugar level, tells cells to absorb glucose

25
Q

Glucagon

A

-Raises blood sugar level, tells liver to release glucose

26
Q

Lipids

A
  • Not true polymers
  • Lots of H
  • Long term energy storage (Primary function)
  • Protection and cushioning
  • Structure (cell membrane)
  • Signalling (enzymes)
27
Q

Fats/Oils

A

Subunit- triglyceride (glycerol with 3 fatty acids)

  • ester linkage
  • Bent if contain double bond (creates irregular shape, more space b/w molecule, therefore liquid)
28
Q

Saturated Fats

A

Single bonds only
Straight
Solid at room temp
Found in animals

29
Q

Unsaturated fats

A

One or more double bonds
Liquid at room temperature
Found in plants

30
Q

Trans Fats

A

Hydrogens on opposite sides of double bond

31
Q

Cis Fats

A

Hydrogens on same side of double bond

32
Q

Phospholipid

A

Phosphate group replaces third fatty acid
Hydrophillic head, hydrophobic tail
Heads face in, tails face out
Creates membranes in all living things (including organelles)

33
Q

Steroids

A

4 carbon rings

  • Makes cell membrane fliud/flexible
  • Cholesterol- needed in small doses- make hormones, stabalizes cell membranes
34
Q

Waxes

A

Protective coating/cover

35
Q

Proteins

A
  • Makes up most structures in cell, carry out chem processes (enzymes)
  • Monomer is amino acid
36
Q

Amino acid

A

Contains carbox acid group, amino group
20 different a.a.
Body can make 12, other 8 considered essential b/c must be in diet
linked by peptide bonds

37
Q

Denatured

A

3-D shape of protein changed
protein no longer functional
Caused by high temp, extreme pH, reactive chemicals (i.e. Cl)

38
Q

Protein Folding

A

1) Primary Structure- amino acids form polypeptide
2) Secondary Structure- Polypeptide folds into double helix or beta pleated sheet b/c of H bonds
3) Tertiary Structure- double helices and beta pleated sheets fold on themselves (charges groups attracting, hydrophillic/phobis interactions, disulphide bridges form and stabalizes 3D shape
4) Quanternary Structure- Multiple tertiary folded proteins come together to form one big unit i.e. hemoglobin

39
Q

Nucleic Acid

A

Chemical codes store plans for all living things
DNA, RNA
Monomer- Nucleotide

40
Q

Nucleotide

A

5 C sugar (ribose), phosphate, N base

link together with 3,5-phosphodiester linkage

41
Q

Metabolism

A

Sum of all chem reactions in cell
Anabolism- small to big
Catabolism- big to small

42
Q

Enzymes

A

Protein molecules that are biological catalysts
Very specific, hundreds/thousands of different enzymes
-“-ase” i,e lipase
Substrate- molecule that enzyme reacts with
Usually part of long series of linked reactions called metabolic pathway (i.e. photosynthesis)
3D shape determines activity
Region that substrate fits in is active site

43
Q

Induced Fit Model

A

Active site conformed to the substrate, substrate and active site binds with H bonds
Brings a.a. closer to substrate, stresses bonds in substrate, Ea decreases OR adds/removes H+ atoms and acts as a catalytic acid or base

44
Q

Temperatue and Enzymes

A

Functions best at 35-40 degrees for humans
Increase temp- H bond disturbed, shape/ function reduced, disulphide linkage break, protein denatured
Decrease temp- Become more rigid, less able to conform, function reduced
Exception: thermostable exzymes in bacteria in hot deep sea vents resistant to high temp. Used in industry

45
Q

pH and Enzymes

A

Works best at 6-8 (humans)
Exception- pepsin, works best at 2-3
pH can denature enzyme (H bonds disrupted)
Specific pH creates correctly shaped active site
Slight change- function reduce
Extreme changes- denatures, loss of function

46
Q

Cofactors

A

Non protein componenents needs for some enzymes for function

Bind to active site with covalent bonds, bind weakly with substrate

47
Q

Coenzymes

A

Organic non protein cofactor
Derivative of vitamin
Carry molecules from one enzyme to another

48
Q

Competitive Inhibitors

A

Substances that look like substrate and prevent substrate from binding to active site

49
Q

Non competitive inhibitor

A

Attatches to somewhere other than active site and changes shape of active site

50
Q

Allosteric inhibitor

A

Attahces at allosteric site and stabalizes inactive form of enzyme

51
Q

Allosteric activator

A

Stabalizes protein conformation

keeps active site open

Biology (3 decks)

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