BMS week 1 Flashcards
types of non covalent bonds
no share of electrons
1. hydrogen bonds
2. hydrophobic forces
3. ionic (salt bridges Na+ Cl-)
4. van der Waals (dipole dipole)
bond in which electrons are shared and is the strongest type of bond
covalent bond
types of covalent bonds
polar- unequal sharing of electrons (delta + and delta -)
non polar- equal sharing of electrons
monosaccharides: components and examples
hydroxy, aldehyde or ketone
-cyclic or linear
-i.e. glucose
- (CH2O)n
amino acid component
amino group, carboxylic acid group, R group
nucleotide components
-phosphate
-5 carbon sugar
-nitrogenous base (purine or pyrimidines)
types of nitrogenous bases (purine and pyrimidines)
purines: 2 rings: adenine and guanine
pyrimidines: 1 ring: uric, thymine and cytosine
fatty acids
unsaturated= 1+ double bonds
saturated= no double bonds
-amphipathic (hydrophilic + hydrophobic)
-i.e phospholipid bilayer
bonds formed between monosaccharides
glycosidic bonds to make disaccharides or polysaccharides
functional group
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
components of triglyceride
glycerol + 3 fatty acids chains = triglyceride
-ester linkage
bonds for amino acids
peptide bonds
-for dipeptide via 2 amino acids joining; remove H2O
nucleotides form nucleic acids to create which structures and via which bonds?
form DNA and RNA via phosphodiester bonds
-5’ and 3’ hydroxyls of 2 adjacent sugars form a double ester with phosphoric acid
what are the components of ATP? (nucleotide)
3 phosphate groups, one ribose sugar, one adenine (nitrogenous base)
essential amino acids
any (arginine- infants)
help (histamine- infants)
in (isoleucine)
learning (leucine)
these (threonine)
little (lysine)
molecules (methionine)
proves (phenylalanine)
truly (tryptophan)
valuable (valine)
branch chain amino acids
leucine
isoleucine
valine
non polar side chains
glycine
alanine
valine
leucine
isoleucine
phenylalanine
tryptophan
methionine
proline
polar side chains
serine
threonine
tyrosine
asparagine
glutamine
cysteine
negatively charged side chains
aspartic acid (aspartate)
glutamic acid (glutamate)
positively charged side chains
histidine
lysine
arginine
@ph of 7 amino acids are:
zwitterions
amphoteric
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+)
anabolic vs catabolic
anabolic: make other amino acids
catabolic: breakdown for energy, CAC
–> release nitrogen to make purine, pyrimidine, urea, heme
pKa > pH
pKa < pH
pKa > pH: then will be COO-
pKa < pH: then will be COOH (protonated form)
enzyme class (reaction example and enzyme name examples): oxidoreductase
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)