Exam 1 Flashcards

(72 cards)

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
Hydrophobic interactions occured because?
Water is polar and excludes nonpolare molecules and groups
26
What is the principal that guides biomolecular interactions that characterize a living state?
Molecular recognition through structure complementarity
27
Biomolecular recognition is mediated by what?
Weak chemical forces
28
Weak forces can be influenced by what environmental factors?
PH, Temp, Salinity
29
PH can change the ____ of functional groups
Protonation states
30
Why are living systems subject to a narrow range of physical conditions?
Weak interactions are subject to change with the physical conditions of the environment
31
If the physical conditions of weak interactions change what happens?
Macromolecules denature and lose function
32
Using enzymes prevents what?
Prevents massive changes in temp, ionic strength, and ph
33
What is a collective set of enzymes called that break down or produce energy in steps called?
A metabolic pathway
34
What are the 2 important things catalysts do?
They don't change the thermodynamic components of a reaction and they only influence the reaction rates
35
What are enzymes?
Enzymes are engines that change one thing into another.
36
What are 4 unusual properties of water?
High boiling point High melting point Hight heat of vaporization High surface tention
37
What makes water polar?
It's bent structure
38
Is water a H donor or an H acceptor
Water is both a donor and an acceptor
39
How many bonds does water have the potential to make?
4 binds but prefers 2
40
On what atoms does hydrogen bonds form?
Form on highly electronegative atoms with a hydrogen attached to a highly electronegative atom.
41
Why is ice less dense then liquid water?
Water makes fewer hydrogen bonds(2) then ice does(4) resulting in more dense liquid
42
What can make a hydrogen shell. What is that?
Where water molecules surrounded ionic atoms. (Dissolve)
43
Water can dissolve what kind of bonds and molecules?
Ionic bonds and polar molecules
44
Non polar molecules do what to water?
Organizes it around the non polar molecules increasing order and reducing entropy.
45
What actions do non polar molecules take in water to order it?
They aggregate together and force water to form a clathrate cage around them.
46
What is an amphophilic molecule ?
A molécule that has both polar and non polar regions and interacts favorable with both polar and non polar environments
47
When a strong electrolyte disassociates in water what will the Ka be?
A large number
48
Upon weak electrolyte disassociation in water the Ka will be what?
A small number
49
What is the formula for acid disassociation constant?
Ka = [H+][A-]/[HA]
50
At what range are buffers reliable?
Within one pH unit of their pKa
51
What does lysozyme cleave
Links between carbohydrates in bacterial cell walls
52
What buffer system is extracellular?
Bicarbonate/ carbonic acid buffer system
53
What buffer systems are used intracellularly (2)
Phosphate buffer system Histidine buffer system
54
What does the bicarbonate buffering system buffer?
Buffers blood pH
55
The + amino group and the - carboxyl group make amino acids what ion type?
A zwitterion
56
When a peptide bond forms between 2 amino acids, what kind of reaction occurs?
A dehydration rxn
57
What causes the plainer configuration of a amino acid chain
The partial double bond character of the N-Co bond
58
Short polymers of amino acids are called what?
Peptides
59
One kind of poly peptide chain is called what?
Homomultimer
60
2 or more kinds of poly peptide chains are called
Hetero multimeter
61
What are the three protein classes?
Fibrous, globular, membrain
62
What is a primary structure
Amino acid sequence
63
What is a secondary structure
Local structure stable by hydrogen bonds
64
What is a tertiary structure
Three dimensional protein shape
65
What is a quaternary structure
Multiple protein subunits that make up a structure
66
What 2 structures form within a secondary protein structure?
Alpha helix and beta sheets
67
In what ways can proteins be purified
Solubility With isoelectric point Salting in and out Column chromatography
68
What types of column chromatography are there?
Affinity columns Ion exchange Size exclusion
69
What is FPLC used for?
Large protein purification
70
What is HPLC used for?
Separation of small molecules (individual amino acids)
71
What kind of electrophoresis is there?
SDS page Isoelectric focusing 2d gel
72
What are the steps in Sanger sequencing?
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