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Biochem 1 > Exam 1 > Flashcards

Exam 1 Flashcards

1
Q

What is biochemistry?

A

The study of biomolecules

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2
Q

What are the 4 biomolecules studied in biochemistry?

A

Carbohydrates, protein’s, lipids, and nucleic acids

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3
Q

What are the 4 most important atomic elements in biochemistry?

A

H, O, C, N

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4
Q

What properties of HOC and N makes them so appropriate for life?

A

Their ability to form covalent bonds by electron pair sharing

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5
Q

What are the order of building blocks to make a cell (5)

A

Inorganic precursors–>Métabolites–> micromolecules and membranes–> Organelles–> cells

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6
Q

The most important characteristic of living organisms is?

A

They actively engage in energy transformation

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7
Q

Most common energy carrying molecules (2)

A

ATP and NADP

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8
Q

How is the energy from ATP accessed?

A

By removing one or more phosphate group.

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9
Q

How is the energy from NADPH accessed?

A

A proton transfer

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10
Q

Chains of amino acids make what polymer.

A

Proteins

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11
Q

Chains of monosaccharides make what polymer?

A

Polysaccharides

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12
Q

Chains of nucleotides make what polymer?

A

Nucleic acids

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13
Q

Micromolecules have a “sense”. What does this mean

A

There is a direction they link into. They have directionality

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14
Q

What holds all macromolecules together

A

Weak forces.

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15
Q

How do weak forces influence macromolecules?

A

Influence structure and behaviors

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16
Q

What are the 4 weak forces that act on macromolecules?

A

-van der Waals force
-hydrogen bonds
-ionic interactions
-hydropgobic interactions

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17
Q

Weak forces can hold molecules together but are not strong Enough to hold ___ together

A

Atoms. Covalent bonds hold atoms together

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18
Q

What are Van Der Waals Forces?

A

An instantaneous asymmetry in the charge of an atom that induces complementary asymmetry in nearby electrons of atoms

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19
Q

What is the vander Waals distance?

A

He minimal distance molecules can be near each other before they are repealed by their size and electronegativity

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20
Q

The net effect of the vanderwaals force is great when?

A

There is a large surface area for it to act upon

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21
Q

When do hydrogen bonds form?

A

When a electronegative atom pulls the electrons from the rest of the atom causing partial positive and negative charges

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22
Q

What are ionic interactions?

A

The attractive forces between fully but oppositely charged structures

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23
Q

3 types of ionic/ electrostatic interactions

A

-Fully but oppositely charges attract
-perminant dipoles
-induced dipoles that are cause by the environment

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24
Q

“burying of non polar regions of macromolecules are caused by what weak force?

A

Hydrophobic interactions

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25
Q

Hydrophobic interactions occured because?

A

Water is polar and excludes nonpolare molecules and groups

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26
Q

What is the principal that guides biomolecular interactions that characterize a living state?

A

Molecular recognition through structure complementarity

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27
Q

Biomolecular recognition is mediated by what?

A

Weak chemical forces

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28
Q

Weak forces can be influenced by what environmental factors?

A

PH, Temp, Salinity

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29
Q

PH can change the ____ of functional groups

A

Protonation states

30
Q

Why are living systems subject to a narrow range of physical conditions?

A

Weak interactions are subject to change with the physical conditions of the environment

31
Q

If the physical conditions of weak interactions change what happens?

A

Macromolecules denature and lose function

32
Q

Using enzymes prevents what?

A

Prevents massive changes in temp, ionic strength, and ph

33
Q

What is a collective set of enzymes called that break down or produce energy in steps called?

A

A metabolic pathway

34
Q

What are the 2 important things catalysts do?

A

They don’t change the thermodynamic components of a reaction and they only influence the reaction rates

35
Q

What are enzymes?

A

Enzymes are engines that change one thing into another.

36
Q

What are 4 unusual properties of water?

A

High boiling point
High melting point
Hight heat of vaporization
High surface tention

37
Q

What makes water polar?

A

It’s bent structure

38
Q

Is water a H donor or an H acceptor

A

Water is both a donor and an acceptor

39
Q

How many bonds does water have the potential to make?

A

4 binds but prefers 2

40
Q

On what atoms does hydrogen bonds form?

A

Form on highly electronegative atoms with a hydrogen attached to a highly electronegative atom.

41
Q

Why is ice less dense then liquid water?

A

Water makes fewer hydrogen bonds(2) then ice does(4) resulting in more dense liquid

42
Q

What can make a hydrogen shell. What is that?

A

Where water molecules surrounded ionic atoms. (Dissolve)

43
Q

Water can dissolve what kind of bonds and molecules?

A

Ionic bonds and polar molecules

44
Q

Non polar molecules do what to water?

A

Organizes it around the non polar molecules increasing order and reducing entropy.

45
Q

What actions do non polar molecules take in water to order it?

A

They aggregate together and force water to form a clathrate cage around them.

46
Q

What is an amphophilic molecule ?

A

A molécule that has both polar and non polar regions and interacts favorable with both polar and non polar environments

47
Q

When a strong electrolyte disassociates in water what will the Ka be?

A

A large number

48
Q

Upon weak electrolyte disassociation in water the Ka will be what?

A

A small number

49
Q

What is the formula for acid disassociation constant?

A

Ka = [H+][A-]/[HA]

50
Q

At what range are buffers reliable?

A

Within one pH unit of their pKa

51
Q

What does lysozyme cleave

A

Links between carbohydrates in bacterial cell walls

52
Q

What buffer system is extracellular?

A

Bicarbonate/ carbonic acid buffer system

53
Q

What buffer systems are used intracellularly (2)

A

Phosphate buffer system
Histidine buffer system

54
Q

What does the bicarbonate buffering system buffer?

A

Buffers blood pH

55
Q

The + amino group and the - carboxyl group make amino acids what ion type?

A

A zwitterion

56
Q

When a peptide bond forms between 2 amino acids, what kind of reaction occurs?

A

A dehydration rxn

57
Q

What causes the plainer configuration of a amino acid chain

A

The partial double bond character of the N-Co bond

58
Q

Short polymers of amino acids are called what?

A

Peptides

59
Q

One kind of poly peptide chain is called what?

A

Homomultimer

60
Q

2 or more kinds of poly peptide chains are called

A

Hetero multimeter

61
Q

What are the three protein classes?

A

Fibrous, globular, membrain

62
Q

What is a primary structure

A

Amino acid sequence

63
Q

What is a secondary structure

A

Local structure stable by hydrogen bonds

64
Q

What is a tertiary structure

A

Three dimensional protein shape

65
Q

What is a quaternary structure

A

Multiple protein subunits that make up a structure

66
Q

What 2 structures form within a secondary protein structure?

A

Alpha helix and beta sheets

67
Q

In what ways can proteins be purified

A

Solubility With isoelectric point
Salting in and out
Column chromatography

68
Q

What types of column chromatography are there?

A

Affinity columns
Ion exchange
Size exclusion

69
Q

What is FPLC used for?

A

Large protein purification

70
Q

What is HPLC used for?

A

Separation of small molecules (individual amino acids)

71
Q

What kind of electrophoresis is there?

A

SDS page
Isoelectric focusing
2d gel

72
Q

What are the steps in Sanger sequencing?

A
  1. Separation of peptide chains
  2. Cleave disulfide bridges
  3. N and C terminal analysis
  4. Fragmentation of peptide chain
  5. Reconstruction of amino acid sequence

Biochem 1 (2 decks)

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