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BMB 507 Exam 1 | Questions and Answers

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BMB 507 Exam 1 | Questions and Answers What does pH represent in relation to hydrogen ions? pH is the negative logarithm of the hydrogen ion concentration, expressed as pH = -log{H+}. What is the significance of pKa in relation to ionization? pKa is the pH at which a molecule is 50% ionized, indicating the strength of an acid. How does the dielectric constant affect pKa modulation? A lower dielectric constant increases electrostatic attraction, making it easier for charges to 'see each other' and thus increasing pKa. What role do hydrogen bonds play in pKa modulation? Hydrogen bonds can increase the pKa of acidic groups. How does temperature influence the pH of buffers? The pH of some buffers decreases as temperature increases. What is the effect of a hydrophobic environment on acidic side chains? In a hydrophobic environment, acidic side chains prefer to be uncharged, raising their pKa. What is the mechanism of aspartyl proteases? Aspartyl proteases use an acid-base mechanism involving two conserved aspartic acid residues in their active site to break peptide bonds. The pKa of the active site is 3.8, so most aspartyl proteases work best at low pHs hydrophobic amino acids alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, tryptophan, cysteine, glycine hydrophilic amino acids lysine, arginine, histidine, aspartate, glutamate, serine, threonine, asparginine, glutamine hydrophilic basic amino acids lysine, arginine, histidine hydrophilic acidic amino acids aspartate, glutamate hydrophilic amino acids with uncharged r groups serine, threonine, asparginine, glutamine amphipathic amino acids proline alanine ala, a hydrophobic Valine val, v hydrophobic isoleucine ile, i hydrophobic leucine leu, l hydrophobic methionine met, m hydrophobic phenylalanine Phe, F hydrophobic Tyrosine tyr, y hydrophobic tryptophan trp, w hydrophobic cysteine cys, c hydrophobic can form disulfide bonds between two cysteines to stabilize extracellular proteins glycine gly, g hydrophobic lysine lys, k basic hydrophilic Arginine arg, r basic hydrophilic aspartate asp, d acidic hydrophilic glutamate glu, e acidic hydrophilic serine ser, s hydrophilic polar with uncharged r groups threonine thr, t hydrophilic polar with uncharged R groups asparginine asn, n hydrophilic polar with uncharged R groups glutamine gln, q hydrophilic polar with uncharged R groups proline pro, p, hydrophobic and hydrophilic can also be found in cis confirmation due to steric hinderance of ring What are the characteristics of alpha helices in protein structure? Alpha helices are right-handed, counter clockwise and form a coiled structure. What distinguishes parallel from antiparallel beta strands? In parallel beta strands, all strands run in the same direction; in antiparallel strands, they run in opposite directions with hairpin turns. What is the Rossmann fold made of? The Rossmann fold consists of alternating beta strands and alpha helices, forming a concave active site that binds nucleotides.

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BMB 507
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Voorbeeld van de inhoud

BMB 507 Exam 1



What does pH represent in relation to hydrogen ions?
pH is the negative logarithm of the hydrogen ion concentration, expressed as pH = -
log{H+}.

What is the significance of pKa in relation to ionization?
pKa is the pH at which a molecule is 50% ionized, indicating the strength of an acid.

How does the dielectric constant affect pKa modulation?
A lower dielectric constant increases electrostatic attraction, making it easier for
charges to 'see each other' and thus increasing pKa.

What role do hydrogen bonds play in pKa modulation?
Hydrogen bonds can increase the pKa of acidic groups.

How does temperature influence the pH of buffers?
The pH of some buffers decreases as temperature increases.

What is the effect of a hydrophobic environment on acidic side chains?
In a hydrophobic environment, acidic side chains prefer to be uncharged, raising their
pKa.

What is the mechanism of aspartyl proteases?
Aspartyl proteases use an acid-base mechanism involving two conserved aspartic acid
residues in their active site to break peptide bonds. The pKa of the active site is 3.8, so
most aspartyl proteases work best at low pHs

hydrophobic amino acids
alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, tryptophan,
cysteine, glycine

hydrophilic amino acids
lysine, arginine, histidine, aspartate, glutamate, serine, threonine, asparginine,
glutamine

hydrophilic basic amino acids
lysine, arginine, histidine

hydrophilic acidic amino acids
aspartate, glutamate

, hydrophilic amino acids with uncharged r groups
serine, threonine, asparginine, glutamine

amphipathic amino acids
proline

alanine
ala, a
hydrophobic

Valine
val, v
hydrophobic

isoleucine
ile, i
hydrophobic

leucine
leu, l
hydrophobic

methionine
met, m
hydrophobic

phenylalanine
Phe, F
hydrophobic

Tyrosine
tyr, y
hydrophobic

tryptophan
trp, w
hydrophobic

cysteine
cys, c
hydrophobic
can form disulfide bonds between two cysteines to stabilize extracellular proteins

glycine
gly, g
hydrophobic

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BMB 507
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