Review from Test 1 Flashcards

1
Q

What is bacterial transformation?

A

the uptake of foreign genetic material by bacteria

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2
Q

Frederick Griffith demonstrated bacterial transformation when

A

heat-killed pathogenic bacteria were able to share genetic information with non-pathogenic bacteria

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3
Q

What is Chargaff’s rule?

A

The ratio of adenine to thymine is always 1:1, and the ratio of guanine to cytosine is always 1:1

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4
Q

What are the three parts of a nucleotide?

A

Nitrogenous base, phosphate group, deoxyribose or ribose sugar

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5
Q

What was the main objective of the experiments conducted by Avery, MacLeod, and McCarthy?

A

Identifying the genetic material responsible for bacterial transformation

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6
Q

What are purines?

A

double-ring nitrogenous bases

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7
Q

What is the name of the covalent bond that holds two nucleotides together?

A

Phosphodiester bond

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8
Q

What is the backbone of DNA and RNA made of?

A

sugar and phosphate

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9
Q

Which of the following represents the flow of information in the Central Dogma of Biology?

A

DNA–RNA–Protein

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10
Q

Which part of an amino acid varies among different amino acids and determines their unique properties?

A

side chain (R-group)

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11
Q

Which of the following is NOT a function of protein?

A

Energy

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12
Q

What information is stores in DNA?

A

The information for the primary sequence of amino acids in polypeptides

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13
Q

Which of the following factors can cause a protein to unfold?

A

changes in pH, changes in solute concentration, changes in temperature

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14
Q

Name the bases of DNA

A

Adenine, Cytosine, Guanine, and Thymine

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15
Q

Name the bases of RNA

A

Adenine, Cytosine, Guanine, and Uracil

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16
Q

Name the five- carbon sugar in DNA

A

deoxyribose

17
Q

Name the five-carbon sugar in RNA

18
Q

Number the strands (# of sugar-phosphate backbones) in DNA

19
Q

Number the strands (# of sugar-phosphate backbones) in RNA

20
Q

Molecules/ functional groups involved in primary structures

A

linear sequence of amino acids

21
Q

Name of bonds holding primary structure of folding together

A

Peptide bonds

22
Q

Description of primary structure

A

Amino acids’ unique sequence in a polypeptide chain

23
Q

Molecules/ functional groups involved in secondary structures

A

alpha helices and beta sheets

24
Q

Name the bonds holding secondary structure of folding together

A

hydrogen bonds

25
Q

Description of secondary structure

A

of proteins refers to the local folding patterns within a polypeptide chain

26
Q

Molecules/functional groups involved in tertiary structures

A

protein represents its three-dimensional conformation, a determinant of its functionality

27
Q

Name the bonds holding tertiary structures of folding together

A

hydrophobic interactions, hydrogen bonds, disulfide bridges, and ionic bonds

28
Q

Description of tertiary structure

A

not static; proteins can undergo conformational changes in response to environmental cues or interactions with other molecules

29
Q

The quaternary structure of a protein is created by the interaction of multiple

A

polypeptides