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Biochem (2016) > Lists > Flashcards

Lists Flashcards

1
Q

What are the 4 main groups of biomolecules?

A

1) Proteins
2) Lipids
3) Carbs
4) Nucleic acids

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2
Q

What the 2 types of metabolism?

A

1) Catabolism - breaking down

2) Anabolism - building up

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3
Q

What are the 5 types of biochemical transformations?

A

1) Group transfer
2) Redox
3) Rearrangement
4) Cleavage
5) Condensation

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4
Q

Which amino acids are non-polar?

A

1) Glycine
2) Alanine
3) Valine
4) Leucine
5) Isoleucine
6) Proline
7) Methionine

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5
Q

Which amino acids are aromatic?

A

1) Phenylalanine
2) Tyrosine
3) Tryptophan

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6
Q

Which amino acids are polar and uncharged?

A

1) Serine
2) Threonine
3) Cysteine
4) Asparagine
5) Glutamine

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7
Q

Which amino acids are negative at pH 7?

A

1) Aspartate

2) Glutamate

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8
Q

Which amino acids are positive at pH 7?

A

1) Lysine
2) Arginine
3) Histidine

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9
Q

What are the 4 levels of protein structure? Describe each level

A

1) Primary - amino acid sequence
2) Secondary - conformational patterns of polypeptide chain, stabilized by H bonds
3) Tertiary - 3D structure
4) Quaternary - interaction of 2 or more globular polypeptides

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10
Q

What does Sanger protein sequencing involve?

A

1) Hydrolysis of the polypeptide
2) Separating the small fragments and determining AA sequence
3) Alignment of the small sequences to generate the complete sequence

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11
Q

What are the determining features of the alpha-helix?

A

1) Peptide bond has planar or double bond character
2) H bonds between every 4th AA
3) R groups point away from the helix

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12
Q

What are features that disrupt the alpha-helix?

A

1) Electrostatic repulsion
2) Bulky R-groups
3) Small residues (favour conversion to beta)
4) Proline in the middle of the helix b/c it can’t become planar

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13
Q

What are characteristics of a beta-sheet?

A

1) Peptide bonds are planar
2) H-bonds form between residues in adjacent strands
3) Usually small R-groups

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14
Q

What are stabilizing features of a proteins tertiary structure?

A

1) Hydrophobic effect
2) Disulfide bonds
3) Electrostatic/ionic interactions
4) H-bonds
5) Metal chelation

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15
Q

What categories can proteins be purified into?

A

1) Charge
2) Size
3) Solubility
4) Affinity for materials

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16
Q

What are the classifications of enzymes and what do they do?

A

1) Oxidoreductases - transfer electrons as H or H-
2) Transferases - transfer groups between molecules
3) Hydrolases - add functional groups to water
4) Lyases - form double bonds
5) Isomerases - isomerize by group transfer
6) Ligases - form C-C, C-S, C-O, and C-N bonds

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17
Q

What are some effects of ES formation?

A

1) Increase in energy
2) Decrease in entropy
3) Desolvation
4) Induced fit
5) Alignment of groups that must react

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18
Q

How does an enzyme recognize and bind a substrate?

A

1) Shape consistency or fit
2) Electrostatic consistency
3) Thermodynamic consistency

19
Q

What are uses of binding energy?

A

1) Entropy reduction
2) Desolvation
3) Strain reduction

20
Q

What are types of enzyme specificity?

A

1) Optical (chiral)
2) Geometric
3) Diastereometric

21
Q

What are the functions of carbohydrates?

A

1) Energy transport and storage
2) Structural
3) Information

22
Q

What are the 2 types of starch?

A

Amylose and amylopectin

23
Q

What are the 2 structural polysaccharides?

A

Cellulose and peptidoglycan

24
Q

What are the functions of nucleotides?

A

1) Precursors of RNA and DNA
2) High energy sources
3) Regulatory signals
4) Coenzymes
5) High energy intermediates in metabolism

25
Q

What are the major types of RNA found in cells?

A

1) Messenger RNA
2) Transfer RNA
3) Ribosomal RNA
4) Micro RNA

26
Q

What are the 5 common mutations in DNA?

A

1) Deamination of C -> U
2) Depurination
3) UV light
4) Oxidative damage
5) Chemicals and mutagenic agents

27
Q

What are the major biological roles of lipids?

A

1) Components of membranes
2) Storage form of carbon and energy
3) Insulation barriers
4) Protective coatings
5) Precursors of other substances
6) Some vitamins and hormones

28
Q

What are properties of fatty acids?

A

1) pKa ~ 4.5-5.0
2) Melting point increases with increasing chain length
3) Solubility - water-soluble up to C6 and then only in non-polar solvents
4) Amphipathic
5) Structure - formation of micelles

29
Q

What are the 2 main types of lipids?

A

Storage and membrane

30
Q

What are properties of triacylglycerols?

A

1) Melting point increases with chain length and with decreasing unsaturation
2) Triglycerides are most abundant family of lipids
3) Fat has 2x more energy per unit mass
4) Insulation
5) Buoyancy

31
Q

What are the types of membrane lipids?

A

1) Glycerophospholipids

2) Sphingolipids

32
Q

What are the types of sphingolipids?

A

1) Sphingomyelins
2) Glycosphingolipids
3) Gangliosides

33
Q

What are the functions of biomembranes?

A

1) Define cell boundaries
2) Regulate traffic in and out
3) Compartmentalize internal space
4) Organize complex reaction sequences
5) Central to energy conservation and cell to cell communication

34
Q

What are the 2 different membrane proteins?

A

Peripheral and integral membrane proteins

35
Q

What are the functions of membrane proteins?

A

1) Structural
2) Transport proteins
3) Enzyme
4) Receptor proteins

36
Q

What are the classes of integral membrane proteins?

A

1) Traverse membrane as single alpha-helix
2) Traverse membrane as 4-12 alpha-helices
3) 8-16 beta-strands form a giant beta-barrel

37
Q

What are the classes of carriers across membranes?

A

1) Uniport
2) Symport
3) Antiport

38
Q

What are the 2 laws of thermodynamics?

A

1) Energy is neither created nor destroyed

2) Entropy of the universe is always increasing b/c it is favourable

39
Q

How are electrons transferred?

A

1) Directly
2) As H atoms
3) Part of a hydride ion (:H-) which has 2 electrons
4) Direct combination with oxygen

40
Q

What are common electron carriers?

A

1) NAD+
2) NADP+
3) FAD
4) FMN

41
Q

How does ATP retain energy and why does hydrolysis release the energy?

A

1) Relief of charge repulsion
2) More resonance forms of ADP + Pi than of ATP
3) When hydrolysis occurs, ADP immediately dissociates one more proton which contributes to the negative delta G
4) Hydrolysis products are solvated by water molecules, further stabilizing products

42
Q

Which processes can produce ATP?

A

1) Substrate level phosphorylation
2) Oxidative phosphorylation
3) Photophosphorylation

43
Q

What are the electron carriers involved in the electron transport chain?

A

1) Coenzyme Q (ubiquinone)
2) Cytochromes
3) Fe-S proteins

44
Q

What are the various complexes in the electron transport chain?

A

1) NADH dehydrogenase
2) Succinate dehydrogenase
3) UQ-Cyt c oxidoreductase
4) Cytochrome oxidase

Biochem (2016) (8 decks)

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