Old MCQs Flashcards
do D-glucose and D-fructose have different chemical formulae?
no
what conformation is most stable for the 4 bases?
the chair conformation
how many bases per turn does the DNA double helix contain?
around 10
can RNA secondary structures include base pairs other than A-T and C-G?
yes
how is the base joined to the ribose in nucleic acids?
via an N-glycosidic bond
what catalytic triad does the specificity pocket of serine proteases contain?
Ser-His-Asp
can histidine act as an acid and a base in enzyme mechanisms?
no
what amino acids are exclusively ketogenic?
lysine and leucine
which amino acids are commonly phosphorylated?
tyrosine and threonine
which amino acids are found in collagen repetitive sequences?
proline and glycine
what is a gel based method to detect the presence of a specific protein in a cell extract?
Western blot
what method is used to find new protein interactions?
coimmunoprecipitation
what method is used to determine the total protein concentration in a sample?
Bradford assay
what sidechains are cell surface oligosaccharides attached to?
serine, threonine, glutamine
do fructose and glucose have the same number of carbon atoms?
yes
do fructose and glucose have a different number of carbon atoms?
no
what does stereochemistry at the anomeric carbon determine?
the shape of polysaccharides
what is the reducing end of a sugar formed by?
the anomeric carbon
what is as accurate as using a Lineweaver Burk plot?
estimation of Km and Vmax from a direct rate vs [S] plot
how many polypeptides is insulin made from?
2
what does insulin stimulate in the adipose tissue?
lipogenesis
what is insulin produced by?
pancreatic beta cells
what does insulin promote in muscle?
glycogen synthesis
how do competitive inhibitors affect Km and Vmax?
affect Km, leave Vmax unchanged
what does the serine protease oxyanion hole do?
stabilises the transition state
what do Asp proteases cleave next to?
aspartic acid residues
can enzymes form covalent bonds with reaction intermediates?
yes
what does rotation around the alpha-carbon in proteins allow?
the protein backbone to fold
do all sugars have a reducing end?
no
is deoxyribose in DNA in the L form?
no
which amino acid is most positively charged at pH 7?
arginine
which amino acid has a side chain attached to sugars in N-linked oligosaccharides?
aspartic acid
which amino acid has an aromatic, hydrophobic sidechain?
Phe
what does the Greek key motif describe?
how 4 beta-strands are packed together
do secondary structures always maximise side chain hydrogen bonds?
no
what are the 2 nucleotides in NAD and FAD connected by?
5’-3’ phosphodiester bonds
what is the pantothenate?
vitamin precursor for a cofactor essential for acyl transfer
are prosthetic groups integral to the protein they’re attached to?
yes
which amino acids are aromatic?
Tyr, Trp, Phe
which amino acids have side chains that are positive at pH 6?
Asp, Lys, His
which amino acids can be phosphorylated?
Ser, Thr, Tyr
which is stronger: binding between 2 strands of an anti-parallel beta sheet or binding between 2 strands of a parallel beta sheet?
anti-parallel
what can accommodate the linkage between 2 strands of an anti-parallel beta-sheet?
short structural loop called a hairpin
what are beta-sheets and alpha-helices exclusively held together by?
hydrogen bonds
what is scurvy caused by?
reduced hydroxylation of proline residues, weakening collagen fibres
which has a higher Km for glucose: glucokinase or hexokinase?
glucokinase
how many immunoglobulin domains do IgG antibodies consist of?
12
is haem a prosthetic group?
yes
what is the iron atom coordinated within in oxy-haemoglobin?
a porphyrin ring
what does carbon monoxide compete with?
oxygen for binding to the haem groups
what binding kinetics does haemoglobin bind oxygen with?
sigmoidal
which amino acid residues can be glycosylated?
Thr, Asn, Ser
where is most glycogen stored: muscle or liver?
muscle