Short answer
General structure of an alpha amino acid?
Short answer
General structure of an alpha amino acid?
Central alpha carbon bonded to an amino group, a carboxyl group, H, and a variable R group.
MCAT 1A · Amino Acids, Proteins and Enzymes
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Cloze
Nonpolar, aliphatic side chains: [...], [...], [...], [...], [...], [...], [...]. They sit in the protein core.
Cloze
Nonpolar, aliphatic side chains: Gly, Ala, Val, Leu, Ile, Met, Pro. They sit in the protein core.
Hydrophobic effect buries them away from water.
Multiple choice
Side-chain charge of Asp at pH 7.4?
- A. Positive
- B. Negative
- C. Neutral
- D. Zwitterionic only
Multiple choice
Side-chain charge of Asp at pH 7.4?
B. Negative pKa about 3.9, so the carboxylate is deprotonated and negative.
True or false
Nearly all amino acids in human proteins are the L (S) enantiomer.
True or false
Nearly all amino acids in human proteins are the L (S) enantiomer.
True. Cysteine is the exception in CIP label only: it is L but R, because sulfur raises the CH2SH priority.
Real cards from the 1A deck, word for word. Click to flip.
Amino acid general structure and alpha carbonStereochemistry of amino acids (L and D, R and S)Side chain classes: nonpolar, aromatic, polar, acidic, basicOne- and three-letter codesSide chain pKa values and charge at physiological pHTitration curves and isoelectric pointHenderson-Hasselbalch applied to amino acidsSpecial residues: Gly, Pro, Cys, His, MetEssential versus nonessential amino acidsPeptide bond formation, resonance and hydrolysisDisulfide bonds and cystinePrimary structureSecondary structure: alpha helix and beta sheetTurns, loops, phi and psi anglesTertiary structure and stabilizing forcesQuaternary structure and subunitsHydrophobic effect and protein folding thermodynamicsChaperones, misfolding and prions
Fig. 1 · Enzyme kinetics, drawn as you scroll
The inhibition table, in ten seconds of scrolling.
01
Michaelis-Menten
v = Vmax[S] / (Km + [S]). Velocity climbs, then flattens as every enzyme is saturated.
02
Read Km and Vmax
Km is the [S] at half of Vmax. Low Km means tight binding.
03
Competitive
Binds free enzyme at the active site. Apparent Km rises; Vmax unchanged. More substrate wins.
04
Noncompetitive
Binds E and ES equally. Vmax falls; Km unchanged.
05
Uncompetitive
Binds only ES. Km and Vmax both fall, so Lineweaver-Burk lines run parallel.
Try it · 3 sample questions
Do not take our word for it. Take the quiz.
3 real practice questions from the 1A pack, word for word. Pick an answer to see the explanation that ships with it.
0 of 3 answered
Q1What is the approximate net charge of the tripeptide Lys-Asp-Gly at pH 7.4?
B. At pH 7.4 the free N-terminal amine is +1, the Lys side chain is +1, the Asp side chain is -1, and the free C-terminal carboxylate is -1, for a net charge of 0. Answering +1 or +2 forgets one or both negative groups, and -1 forgets the N-terminus.
Q2Why does the peptide bond not rotate freely?
D. Delocalization of the nitrogen lone pair onto oxygen makes the amide plane rigid. A hydrogen bond, ionic bond, or disulfide would be a different type of interaction and would not describe the amide linkage.
Q3An enzyme transfers an amino group from one molecule to another. Which EC class?
A. Group transfer defines EC 2 (transferases), as with aminotransferases. Ligases join molecules using ATP, lyases cleave without water or redox, and isomerases rearrange one molecule.
That was 3 questions. This pack has 53, plus 423 flashcards.
See the packFig. 2 · What is inside a pack (1A shown)
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- 01Amino acids
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