Ch 1 - Bio Chemistry Flashcards

1
Q

What elements do Carbohydrates and proteins have in common?

What element separates out proteins from carbs?

A

C H N O

C H N O S - Sulfur

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2
Q

What are the polysacharrides of starch

A

amylose - 1-4 glycosidic linkages of Glucose

amylopectin - 1-4 glycosidic linkages and 1-6 glycosidic linkages (Like Glycogen but less branched)

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3
Q

What is a nucleon?

A

Proton or Neutron

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4
Q

Are soluble protein’s electrostatic interactions stronger internally or externally?

A

Internally - The water hydrogen bonds create an solvent shell that weaken the electrostatic interactions

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5
Q

-ΔG means?

A

Spontaneous reaction (exergonic)

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6
Q

+ΔG means?

A

Non-Spontaneous reaction (endergonic)

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7
Q

ΔG = 0 means?

A

The reaction is at equilibrium

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8
Q

Are almost all exothermic reactions spontaneous or non-spontaneous?

A

Spontaneous

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9
Q

-ΔH and +ΔS means what?

A

The reaction will be spontaneous regardless of temperature

ΔG = ΔH - T ΔS

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10
Q

Open System

A

mass and energy can exchange

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11
Q

Closed System

A

allows energy to transfer, but not mass

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12
Q

Isolated System

A

Neither energy nor mass can transfer

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13
Q

Chemotroph

A

Derive free energy from the oxidation of fuel molecules

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14
Q

Biotin

A

Biotin is a cofactor involved in carboxylation and decarboxylation reactions.

Transfers CO2

Used in Glycolysis

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15
Q

S-Adenosylmethionine (SAM)

A

CoFactor involved in CH3 (methyl) group transfers

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16
Q

Explain steric hinderance in Peptide bonds and why it’s significant

A

The bond has about a 40% double bond characteristic and takes on a trans formation. This makes it so the peptide bond is rigid.

17
Q

How man structural isomers would there be for

  • Val
  • Tyr
  • Ala?
A

3! = 321 = 6

18
Q

How man optical isomers would there be for ValTyrAla?

A

N = 3 since each is chiral 2^3 = 8

19
Q

What are the primary, secondary, tertiary, and quaternary structures of proteins?

A

primary: sequence of amino acids held by covalent bonds. This includes the peptide bond and disulfide bond.
secondary: This is the 3D conformation of localized regions caused by hydrogen bonds. (Beta sheets)
tertiary: This is the 3D structure of the entire protein held together by hydrogen bond, disulfide bonds, salt bridges (electrostatic interactions), and van der walls interactions.
quaternary: How different peptide chains interact with all the same interactions as tertiary

20
Q

What is the difference between digestion and denaturing

A

Digestion breaks the primary structure, denaturing only breaks the secondary -> quaternary

21
Q

How does heat work as a denaturing agent?

A

It breaks Hydrogen bonds. It causes the molecules to vibrate too violently.

22
Q

How does radiation work as a denaturing agent?

A

It breaks Hydrogen bonds. It causes the molecules to vibrate too violently.

23
Q

How do detergents work as a denaturing agent?

A

affects salt bridges and H bonds

24
Q

How do acids / bases work as a denaturing agent?

A

affects salt bridges and H bonds

25
Q

How do salts of Heavy Metals such as Ag+, Hg++, and Pb++ work as a denaturing agent?

A

Bond with SH groups to form precipates as well as acidic amino acids

26
Q

How does Urea work as a denaturing agent?

A

Disrupts hydrogen bond.

27
Q

How many hydrogen bonds do the nucleotides A-T or A-U have?

A

2

28
Q

How many hydrogen bonds do the nucleotides G-C have?

A

3

29
Q

What’s the difference between a nucleotide and a nucleoside

A

A nucleoside is a sugar and N-base. A nucleotide has a phosphate group attached as well on the 5’ OH

30
Q

What makes up the backbone of DNA?

A

The sugar-phosphate complex. The nitrogenous bases make up the middle of DNA.

Phosphodiester bonds between 5’ and 3’ OH on Glucose

31
Q

How are DNA monomers linked?

A

Phosphodiester bonds between the 5’OH of one nucelotide and the 3’ OH of another.