BMS week 1 Flashcards

1
Q

types of non covalent bonds

A

no share of electrons
1. hydrogen bonds
2. hydrophobic forces
3. ionic (salt bridges Na+ Cl-)
4. van der Waals (dipole dipole)

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2
Q

bond in which electrons are shared and is the strongest type of bond

A

covalent bond

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3
Q

types of covalent bonds

A

polar- unequal sharing of electrons (delta + and delta -)
non polar- equal sharing of electrons

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4
Q

monosaccharides: components and examples

A

hydroxy, aldehyde or ketone
-cyclic or linear
-i.e. glucose
- (CH2O)n

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5
Q

amino acid component

A

amino group, carboxylic acid group, R group

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6
Q

nucleotide components

A

-phosphate
-5 carbon sugar
-nitrogenous base (purine or pyrimidines)

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7
Q

types of nitrogenous bases (purine and pyrimidines)

A

purines: 2 rings: adenine and guanine
pyrimidines: 1 ring: uric, thymine and cytosine

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8
Q

fatty acids

A

unsaturated= 1+ double bonds
saturated= no double bonds
-amphipathic (hydrophilic + hydrophobic)
-i.e phospholipid bilayer

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9
Q

bonds formed between monosaccharides

A

glycosidic bonds to make disaccharides or polysaccharides

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9
Q

functional group

A

hydroxyl -OH
sulfhydryl -SH
carbonyl C=O
carboxyl COOH
ester COO
phosphoryl PO3
amino NH2
amido NH2O
methyl CH4
ether
thioester
anhydride
mixed anhydride
phosphoanhydride

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10
Q

components of triglyceride

A

glycerol + 3 fatty acids chains = triglyceride
-ester linkage

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11
Q

bonds for amino acids

A

peptide bonds
-for dipeptide via 2 amino acids joining; remove H2O

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12
Q

nucleotides form nucleic acids to create which structures and via which bonds?

A

form DNA and RNA via phosphodiester bonds
-5’ and 3’ hydroxyls of 2 adjacent sugars form a double ester with phosphoric acid

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13
Q

what are the components of ATP? (nucleotide)

A

3 phosphate groups, one ribose sugar, one adenine (nitrogenous base)

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14
Q

essential amino acids

A

any (arginine- infants)
help (histamine- infants)
in (isoleucine)
learning (leucine)
these (threonine)
little (lysine)
molecules (methionine)
proves (phenylalanine)
truly (tryptophan)
valuable (valine)

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15
Q

branch chain amino acids

A

leucine
isoleucine
valine

16
Q

non polar side chains

A

glycine
alanine
valine
leucine
isoleucine
phenylalanine
tryptophan
methionine
proline

17
Q

polar side chains

A

serine
threonine
tyrosine
asparagine
glutamine
cysteine

17
Q

negatively charged side chains

A

aspartic acid (aspartate)
glutamic acid (glutamate)

17
Q

positively charged side chains

A

histidine
lysine
arginine

18
Q

@ph of 7 amino acids are:
zwitterions
amphoteric

A

zwitterions: no net charge across C and N terminals (R group might be)

amphoteric: acts as acid or base by donating or accepting electrons (i.e. H+)

19
Q

anabolic vs catabolic

A

anabolic: make other amino acids

catabolic: breakdown for energy, CAC
–> release nitrogen to make purine, pyrimidine, urea, heme

20
Q

pKa > pH
pKa < pH

A

pKa > pH: then will be COO-
pKa < pH: then will be COOH (protonated form)

21
Q

enzyme class (reaction example and enzyme name examples): oxidoreductase

A

redox; dehydrogenase (remove hydrogen and donate them to a molecule other than oxygen), oxidase (remove H and donate to oxygen)

-LEO GER (add or lose electrons/ hydrogens)

22
Q

enzyme class (reaction example and enzyme name examples): hydrolase

A

hydrolysis (nucleophilic substitution); phosphatase, ATPase (i.e. hydrolyse ATP to release phosphate group), peptidase, lipase

catalyze hydrolysis reactions (break apart with H2O)
–> H2O acts as nucleophile

23
Q

enzyme class (reaction example and enzyme name examples): transferase

A

group transfer (nucleophilic substitution); kinase (transfer phosphate group from ATP to another non water molecule), polymerase (transfer monomer to a polymer like DNA or RNA), “X”-transferase

-synthesize molecules by catalyzing the transfer group from one molecule to another
-nucleophile: atom with lone electron pair
-electrophile: electron deficient atom
-leaving group: substituted for by nucleophile

-use of “carriers”, add to transfer molecule in place of functional group bc better leaving group i.e. triglyceride formation

24
Q

enzyme class (reaction example and enzyme name examples): lyase

A

condensation; synthase

decarboxylation/elimination; decarboxylase

dehydration/elimination; dehydratase

hydration/addition; hydratase

  1. addition: add molecules across a double or triple bond
  2. elimination: remove atoms to create double bond
  3. condensation: join two molecules, create new C-C bond
25
Q

enzyme class (reaction example and enzyme name examples): isomerase

A

isomerization; mutase, epimerase, racemase

-rearrange group(s) within a molecules, no NET addition or elimination of atoms

  1. mutases: transfer functional groups intramolecularly
  2. epimerases: interconvert groups around an asymmetric carbon in a molecule that has >1 asymmetric carbon
  3. racemases: interconvert groups around an asymmetric carbon in a molecule that has 1 asymmetric carbon (could be isomerization, but not isomerase bc intermediate step)
26
Q

enzyme class (reaction example and enzyme name examples): ligase

A

joining molecules with the use of ATP; synthetase, synthase, “X”-ligase