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From Flashcardlet > biol > Flashcards

biol Flashcards

0
Q

3 main macromolecules

A

Carbohydrates, proteins, nucleic acids

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1
Q

4 main classes of large molecules in living things

A

Carbohydrates, proteins, nucleic acids, lipids

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2
Q

Polymer

A

Long molecule of many similar or identical building blocks linked by covalent bonds

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3
Q

Monomer

A

Small molecules that serve as repeating building blocks for polymers, though some also have other functions of their own.

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4
Q

Enzymes

A

Specialized macromolecules that speed up chemical reactions

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5
Q

Dehydration reaction

A

A reaction in which two molecules are covalently bonded to each other, with the loss of a water molecule.

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6
Q

Hydrolysis

A

Breaking up of a molecule by the addition of water (attaching hydroxyl group to one piece and a hydrogen to the other).

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7
Q

Carbohydrates

A

Macromolecules composed of sugars and polymers of sugars. Includes:
Monosaccharides
Disaccharides
Polysaccharides

Most sugar names end in -ose.

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8
Q

Glucose

A 
Monosaccharide
C6H12O6
Aldose (carboxyl on end)
Hexose (skeleton is 5 C long)
Isomer of fructose
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9
Q

asymmetric carbon

A

A carbon attached to 4 different atoms or groups of atoms.

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10
Q

colloid

A

a stable suspension of fine particles in a liquid

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11
Q

hydroxyl functional group

A

-OH / HO-

Alcohols (specific names tend to end in -ol)

Ex: ethanol

Is polar due to electronegative O

Can form H bonds with water, dissolving organic compounds such as sugars.

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12
Q

carbonyl functional group

A

> CO (w/ dbl bond to O)

Ketones (w/in skeleton)
Aldehydes (@ end of skeleton)

Ex: acetone, simplest ketone
Ex: propanol, an aldehyde

Ketone/aldehyde may be structural isomers (like above)

Also found in sugars: ketoses / aldoses

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13
Q

carboxyl functional group

A

-COOH (dbl to O, single to OH)

Carboxylic acids

Ex: acetic acid (makes vinegar sour)

Acts as acid because it can donate H+ due to OH being so polar

Found in cells in the ionized form w/ 1- charge, called a carboxylic ion.

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14
Q

amino functional group

A

-NH2

Amines

Ex: glycine, which has both amino and carboxyl groups, so called an amino acid.

Acts as a base

Found in cells in ionized form with 1+ charge.

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15
Q

sulfhydryl functional group

A

-SH or HS-

Thiols

Ex: cysteine, important sulfur containing amino

Two sulf’s can covalent bond, stabilizing protein structure (cross-linking)

Cross-linking maintains straight or curly hair

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16
Q

phosphate functional group

A

-OPO3 2- (1 dbl PO, 3 single PO bonds, two w/ neg O charge, and neutral one also bonded to skel)

Organic phosphates

Ex: glycerol phosphate, backbone for phospholipids

Adds neg charge to any molecule it joins (2- from the end, or 1- from inside)

Mol’s w/ phosphate can potentially react w/ water, releasing energy.

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17
Q

methyl functional group

A

-CH3 (can attach to carbon or a diff atom)

Methylated compounds

Ex: 5-Methyl cytidine, component of DNA, modified by adding a methyl group

Adding methyl group to DNA or mol’d bound to DNA affects expression of gene

Their arrangement in male/female sex hormones affects their shape and function

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18
Q

Protein structure: primary

A

Linear chain of amino acids

N-terminus (+H3N), amino

C-terminus (COOH), carboxyl

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19
Q

Protein structure: secondary

A

Regions stabilized by hydrogen bonds between atoms of the polypeptide backbone, forming coils and folds.

Main types:
α helix: coil made by H binding on every 4th amino acid

β pleated sheet: parallel polypeptide chains (β strands) connected by H bonds between backbones

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20
Q

Protein structure: tertiary

A

3D shape stabilized by interactions between side chains (R groups).

  1. Hydrophobic interaction: non polar side chains cluster in the core, held together by van der Waals
  2. H bonds between polar side chains
  3. Ionic bonds between pos and neg charged side chains
  4. Disulfide bridges: covalent bonds between 2 cysteine monomers and their sulfhydryl groups (-SH -> -S-S-)
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21
Q

Protein structure: quaternary

A

Association of two or more polypeptides, forming a functional protein.

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22
Q

denaturation

A

unraveling of a protein’s natural shape due to changes in the surrounding pH, salt concentration, temp, or other aspects.

Because it is misshapen, it is biologically inactive.

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23
Q

chaperonins

A

protein molecules that assist in the proper folding of other proteins.

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24
Q

DNA bases

A

adenine / thymine

guanine / cytosine

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25
Q

RNA bases

A

adenine / uracil

guanine / cytosine

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26
Q

endomembrane system components and functions

A 
nuclear envelope
endoplasmic reticulum 
Golgi apparatus 
lysosomes
various vesicles & vacuoles
plasma membrane

protein synth, transport, metabolism & movement of lipids, detox of poisons.

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27
Q

helicase

A

Enzyme that untwists the double helix at the replication fork

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28
Q

single-strand binding proteins

A

binds to unpaired DNA strands to keep them from re-pairing

29
Q

topoisomerase

A

breaks, swivels, and rejoins DNA strands ahead of replication fork, relieving strain

30
Q

primer

A

short RNA chain, serves as initial nucleotide chain during DNA synthesis. Synthesized by primase.

31
Q

primase

A

enzyme that synthesizes RNA primer

32
Q

nucleoside

A

sugar and a base (no phosphate group)

33
Q

DNA polymerases

A

Catalyze DNA synthesis by adding nucleotides to a preexisting chain.

34
Q

DNA polymerase III

A

Adds a DNA nucleotide to RNA primer, then continues adding nucleotides, complementary to parental DNA template strand.

35
Q

DNA polymerase I

A

Replaces RNA primer between Okazaki fragments with DNA by adding to 3´ end of latest fragment.

36
Q

DNA ligase

A

joins sugar-phosphate backbones of Okazaki fragments into continuous DNA strand

37
Q

mismatch repair

A

enzymatic removal and replacement of incorrectly paired nucleotides

38
Q

nuclease

A

enzyme that cuts DNA (during repair processes)

39
Q

telomeres

A

multiple repetitions of one short nucleotide sequence at the ends of DNA molecules, a buffer zone against gene shortening. Human sequence is TTAGGG

40
Q

telomerase

A

catalyzes the lengthening of telomeres in eukaryotic germ cells.

41
Q

histone

A

Small protein (about 100 amino acids), around which DNA strand is wrapped twice. Four types common in chromatin: H2A, H2B, H3, H4

42
Q

nucleosome

A

a “bead” of DNA wrapped twice around a core of histones (2 pairs each). Amino end (n-terminus) of each histone (the histone tail) extends outward.

43
Q

heterochromatin

A

highly condensed state of centromeres and telomeres in interphase chromatin

44
Q

euchromatin

A

dispersed chromatin (vs compact heterochromatin)

45
Q

nucleotide excision repair

A

process in which nucleases cut out damaged stretches of DNA, which is replaced by polymerase and sealed by ligase.

46
Q

promoter

A

DNA sequence where RNA polymerase attaches and initiates transcription

47
Q

terminator

A

DNA sequence that signals the end of transcription (in bacteria)

48
Q

transcription unit

A

the stretch of DNA that is transcribed

49
Q

start point

A

the nucleotide where RNA synthesis actually begins

50
Q

transcription factors

A

collection of proteins that mediate the binding of RNA polymerase and the initiation of transcription (in eukaryotes). One recognizes the TATA box.

51
Q

transcription initiation complex

A

the whole complex of transcription factors and RNA polymerase II bound to the promoter

52
Q

TATA box

A

a crucial promoter DNA sequence, containing TATA, about 25 nucleotides upstream from the transcriptional start point

53
Q

5´ cap

A

a modified form of a guanine nucleotide added to 5´ end of pre-mRNA molecule after transcription of first 20-40 nucleotides.

54
Q

polymerase II

A

binds to promoter (in prok cells) or transcription factors on the promoter (in euk cells) to form the transcription initiation complex, and begin transcribing DNA to RNA.

55
Q

poly-A tail

A

string of adenine nucleotides (50-250) added to 3’ end of pre-mRNA

56
Q

UTR

A

untranslated region: 5’ UTR and 3’ UTR do not get translated into protein, but have other functions, such as ribosome binding.

57
Q

RNA processing

A

enzymes in euk nucleus modify pre-mRNA before dispatch to cytoplasm: adds 5’ cap and poly-A tail, plus RNA splicing

58
Q

RNA splicing

A

removal of introns, joining of exons, done by spliceosomes (snRNPs + additional proteins)

59
Q

snRNP

A

small nuclear ribonucleoprotein: recognizes splicing sites at the ends of introns

60
Q

ribozymes

A

RNA molecules that function as enzymes, sometimes catalyzing their own excision

61
Q

alternative RNA splicing

A

Genes can give rise to two or more different polypeps, depending on which segments are treated as exons during RNA processing.

62
Q

protein domains

A

discrete structural and functional regions of the protein

63
Q

exon shuffling

A

.

64
Q

spliceosome

A

combo of snRNPs and additional proteins. Interacts with introns, releasing them, and joining together the exons.

65
Q

wobble

A

flexible base pairing at the 3rd codon position between tRNA and mRNA

66
Q

aminoacyl-tRNA synthetase

A

family of related enzymes that match up each tRNA to its specific amino acid

67
Q

frameshift mutation

A

mutation altering the reading frame (caused by nucleotide-pair insertion or deletion)

68
Q

silent mutation

A

Nucleotide-pair substitution with no effect.

69
Q

missense mutation

A

Nucleotide-pair substitution that changes one amino acid into another

70
Q

nonsense mutation

A

Nucleotide-pair substitution that changes an amino acid codon into a stop codon, causing translation to end prematurely.

From Flashcardlet (8 decks)

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