Biochem Qs bank Flashcards
which amino acid is important in the buffering action of proteins at physiological pH values?
histidine
Which of the following is a ketogenic amino acid?
lysine
a protein domain is defined as:
an independent folded structure within a polypeptide with an independent function
in competitive enzyme inhibition, Km:
always goes up
a prosthetic group is defined as:
non-protein component bound to a protein for its activity
sugar acids are monosaccharides that have:
a hydroxyl group oxidised to a carbonyl group
which of these statements are false?
facilitated diffusion requires GTP
pyruvate dehydrogenase is made up of which three enzymes?
pyruvate decarboxylase (PD), dihydrolipoyl dehydrogenase (DD), and lipoamide reductase transacetylase (LRT)
if delta G for a reaction is positive, the reaction is said to be?
endothermic
conversion of phosphoenol pyruvate into pyruvate is the last reaction of glycolysis. This reaction is catalysed by:
pyruvate kinase
an example of peripheral membrane protein is:
spectrin
specialised membrane transport proteins, termed channel proteins:
all of the above
which is a ketogenic amino acid?
lysine
what does the charge relay system consist of?
serine, histidine, and aspartate
how do you work out pH/?
pH=-log10(H+)
which of these enzymes are inhibited by NADH and ATP in the TCA cycle?
alpha ketoglutarate dehydrogenase and isocitrate dehydrogenase
two sources of glucose in the body
diet and liver
ribosomes are…
protein factories
what is the major buffer in saliva?
carbonic acid
which amino acid does not have an asymmetric carbon atom?
glycine
which amino acid causes a bend in the peptide chain?
proline
what is the optically inactive amino acid?
glycine
what happens to enzymes after a reaction
unaltered
the organelle in which complex carbohydrates such as GAGs are synthesised in?
golgi apparatus
what is a zymogen?
inactive enzyme
XXX reduces the enzyme effect but inhibition is 95% reversed when the substrate is increased by 1000 fold. What inhibition is this?
competitive inhibition
what does competitive inhibition do to the Km?
increases it
what is an example of oxidative deamination
glutamate to alpha ketoglutarate and ammonia
where is pyruvate converted to oxaloacetate?
mitochondria
which of the following about protein domains is true:
independent subunits with independent function
which of these amino acids do not have D dextrarotatory right-handed optical isomerism?
glycine
an enzyme with a high Km has a…
low affinity
PDC catalyses the conversion of pyruvate into?
acetyl CoA
what is the linkage for branching in glycogen?
alpha 2–>6
if delta G is close to 0 what affects the reaction?
concentration
which one is not one of the four biologically important organic molecules?
fats
which is a system involved in homeostasis?
endocrine system
porins can be found in:
gram negative cell wall
the carbonic acid concentration in the mouth is approximately
1.3mMol/L
what is an alpha carbon?
carbon to which the amino acid carboxylic groups are attached
the majority of amino acids in the body are
L
the pK value for carboxylic acid is
2.2
the pK value for amino group is
9.4
which is not an example of an aliphatic amino acid?
lysine
example of an aromatic amino acid includes
phenylalanine
which amino acid has a weakly acidic hydroxyl group?
tyrosine
example of an imino acid includes
proline
amino acids carry a
negative charge
which amino acid is not involved in the addition of sugars?
tyrosine
secondary structure of proteins involves
hydrogen bonds
tertiary structure of proteins involves
non-covalent interactions
disulphide bonds can be formed by
cysteine
protein domains are formed in
tertiary structure
keratin is a
fibrous protein
collagen is a
fibrous protein