Week 1 Content - Intro, Buffers, Acid Base Disorders, AA and Proteins, Hb Flashcards
What is considered a volatile acid? How does the body get rid of it?
carbon dioxide - major metabolic acid - it is lost in expiration by the lungs
what are the types of non-volatile acids? How does the body get rid of them?
Inorganic non-volatile acids = sulfuric acid, phosphoric acid
Organic acids = ketone bodies, lactic acid
All lost through the kidneys and urine
amino acids can act as an acid or a base. What is the name for this?
amphoteric
What protein is rich in hisitine side chains?
Hb
How is GABA formed? (aa and mechanism)
glutamate by decarboxylation
How is histamine formed? (aa and mechanism)
histidine by decarboxylation
How is seratonin formed? (aa and mechanism)
tryptophan is hydroxylated and decarboxylated
How are catecholamines formed? (aa and mechanism)
tyrosine is hydroxylated = L-DOPA
L-DOPA is decarboxylated = dopamine = 1st catecholamine!
peptide bonds are typically…
polar and uncharged
denaturing proteins - what breaks hydrogen bonds?
heat, urea, salt
denaturing proteins - what breaks ionic bonds?
strong acids
strong bases
denaturing proteins - what breaks hyrophobic interactions
SDS detergent
denaturing proteins - what breaks/ reduce disulfide bonds?
thiol containing compounds
beta mercaptoethanol (Bme)
2-mercaptoethanol
what actually happens in prions disease?
PrP = PrPsc
the alpha helix is changed to a beta pleated sheet which is strong
“holes in brain”
myoglobin is a…
monomer
hemoglobin is a…
tetramer
What fraction of total hemoglobin is Hb A?
90% alpha 2 beta 2
what fraction of total hemoglobin is Hb F?
< 2%
alpha 2 gamma 2
what fraction of total hemoglobin is Hb A2?
2-5%
alpha 2 delta 2
what fraction of total hemoglobin is Hb A1c?
3-9%
alpha 2 beta 2 - glucose
what are the negative polar aa?
aspartate, glutamate
what are the polar uncharged aa?
thrionine, serine, asparagine, glutamine
what are the positively charged polar aa?
lysine, arginine, and sometimes histidine!
what factors cause a right shift in the ocygen dissocation curve?
decrease O2 affinity = increase in temperature, decrease in pH, increase in PCO2, increase in 2,3 BPG, increase HK, decrease PK
“everything you do with exercise”
with weak acid drugs, what happens if the pH<pK?
absorption in stomach = uncharged form!
with weak basic drugs, what happens if the pH>pK?
absorption in intestine = uncharged form!
what is the primary structure of proteins?
aa sequence
what is the secondary structure of proteins?
alpha helix (with hydrogen bond every 4th aa) and beta pleated sheet)
what is the tertiary structure of protein?
3D conformation of the protein
what is needed for the proper cleavage of insulin?
C-peptide!
what do chaparones do in multimeric proteins?
they facilitate proper folding
what picks up protein mis folding?
ubiquitin
what is the structure common to all amino acids of proteins?
H3C - alpha C - COOH
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R side chain (groups i memorized)
which polar uncharged aa have an OH group?
serine and thrionine
what determines the properties of proteins?
the side chain - structure and function are related
what plays an important role in protein folding and function?
polarity of the side chain
where do the polar aa cluster (hydrophilic)?
on the surface of soluble proteins
where do nonpolar aa cluster (hydrophobic)?
on the surface of membrane proteins
how are proteins and peptides synthesized?
translation of mRNA ot protein
what are covalent bonds and what are some examples?
they are strong and are not meant to be broken unless during protein degradation
peptide bonds between 2 aa
disulfide bonds
what do non covalent bonds do and what are some examples?
they are weaker and specificy protein folding and conformational changes - these weak forces may be additive
hydrophobic forces
hydrogen bonds
ionic bonds
van der walls
how are secondary structures of proteins stabilized?
by hydrogen bonds involving the atoms of peptide bonds
where are the aa side chains in the alpha helix?
they stick out
what is the beta pleated sheet characterized by?
hydrogen bnods perpendicular to peptide bond atoms
aa side chains that alternate above and below plane
when can hydrogen bonds be formed?
between 2 polar uncharged side chains
one charged side chain and one polar side chain (ion dipole attractive force)
what holds the A and B chains of insulin together?
2 inter-chain disulfide bonds
what folds the peptide hormone and is needed for receptor recognition?
the intra-chain disulfide bond
what does myoglobin not have?
beta pleasted sheet
what is myoglibin describes in terms of?
tertiary structure
what is hemoglobin described in terms of?
quaternary structure
what in myoglobin and hemoglobin look almost identical?
the beta chain of hemoblogin and the tertiary structure of myoglobin
what is monomeric mean?
single polypeptide chain - teritary structure description
what does multimeric mean?
more than 1 polypeptide chian - quaternayr structure description
what is homomultimeric?
all chains are the same
what is heteromultimeric
all chains are different
how do the subunits of multimeric proteins (quaternary structure) associate (bonds)
non covalent forces
examples - Hb
what does HSP 70 do?
prevents aggregation of unfolded prtine
what does it mean to denature protien?
3D structure is changed - the peptide backbone is intact - primary structure is good
once denatured you can fix it back
in alzheimer’s disease or prions diseasewhat is the deal with ubiquitin and proteasome?
the diseased proteins are very stable and not picked up - so abnormal proteins accumulate and dammage the brain
the infectious agent in prions disese is what?
a single protein
what are 3 structual fibrous proteins?
collagen, keratin, elastin
what are globular rtansport proteins?
albumin and Hb
how are extracellular proteins stabilized?
disulfide bonds - thats why its in albumin
how are extracellular proteins stabilized?
disulfide bonds - thats why its in albumin
where are hydrophobic forces formed?
between side-chains of branched-chain amino acids. These side chains are nonpolar and they would be normally mainly found inside of a globular protein.
where are hydrophobic forces formed?
between side-chains of branched-chain amino acids. These side chains are nonpolar and they would be normally mainly found inside of a globular protein.
what does Hsp 60 do?
barrel shape and have function of folding and refolding proteins
what does Hsp 60 do?
barrel shape and have function of folding and refolding proteins
