macromolecules part b Flashcards

1
Q

what is a nucleic acid?

A
  • genetic material of the cell (cell fxn, replication, and genetic info)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what monomer makes up nucleic acids and what bonds the monomers together?

A
  • nucleotides (sugar (deoxy or ribo) phosphate backbone and nitrogenous bases)
  • phosphodiester bonds !
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what bonds form between nitrogenous bases of a nucleotide

A

Hydrogen bonds (covalent)`

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what are the three chemical differences between DNA and RNA

A

-sugar used in backbones (deoxyribose or ribose)
- 3D structure (RNA bonds internally, single stranded)
- Uracil pyrimidine base instead of Thymine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

DNA is a directional molecule what does this mean

A

the 3’ (attached to OH group at end of DNA) bonds with the 5’ end (attached to the terminal phosphate) of each strand

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

purines vs pyrimidines

A

PURINES; A&G- one pentose
PYRIMIDINES; T(U)&C- two carbon rings

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

which nitrogenous base bonds with which, and why?

A

G-C and A-T (because purines and pyrimidines are structurally different and are unable to form sufficient bonds within like pairs)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

how are proteins formed

A

amino acids are bonded together by peptide bonds to form linear polypeptide strands which fold and coil into itself to become a protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what are examples of polypeptides

A

hemoglobin, collagen, and insulin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what are the four levels of protein structure? (+ bonds of each)

A

primary: unique order of amino acids (peptide)
secondary: folding of polypeptide (H-bonds b/w carboxyl and amino)
tertiary: overall folded 3D shape of polypeptide [protein formed] (H-bonds, ionic bonds, hydrophobic interactions, disulfide bonds in cystine)
quaternary: multiple polypeptides together (same bonds as tertiary; h, ionic, disulfide, hydrophobic)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

what are polypeptides (structure + fxn)

A

fxn: enzymes, transport &structural proteins, hormones, receptors etc)
structure: long peptide bonded chain of amino acids made up of an amino group, R group, and carboxyl)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what does it mean for polypeptides to be directional?

A

folded chain only bonds carboxyl ends of amino acids to amino ends of others (creating and limiting unique shape)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what are the differences between denaturing and degrading a protein?

A

degrade; permanent damage of primary structure, no fxn left cant be reversed
denature; non permanent damage of secondary, tertiary, and quaternary structures, protein can’t fxn

How well did you know this?
1
Not at all
2
3
4
5
Perfectly