Biochemistry Exam 1 Flashcards
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Questions and Answers

Classify the following molecule: ampipathic?

  • Hydrophobic
  • Hydrophilic
  • Amphipathic (correct)
  • None of the above

Classify the following molecule: hydrophilic?

  • Hydrophobic
  • Hydrophilic (correct)
  • Amphipathic
  • None of the above

Classify the following molecule: hydrophobic?

  • Hydrophobic (correct)
  • Hydrophilic
  • Amphipathic
  • None of the above

What is the pH of 1x(10^-9) M sulfuric acid (H2SO4)?

<p>7 (or slightly less than 7)</p> Signup and view all the answers

How many carbons does this molecule contain?

<p>4</p> Signup and view all the answers

How many hydrogens are present in this molecule?

<p>10</p> Signup and view all the answers

How many of these hydrogens can engage in hydrogen bonding?

<p>0</p> Signup and view all the answers

Which of the following curve shapes corresponds most closely to performing a full titration of the amino acid isoleucine?

<p>Curve D (B)</p> Signup and view all the answers

What letter (A to E) represents the peptide bond that connects the two residues?

<p>C</p> Signup and view all the answers

Which bond(s) A to E do(es) not rotate freely?

<p>C</p> Signup and view all the answers

What amino acid (AA) is repeated here?

<p>Alanine</p> Signup and view all the answers

When the pH is less than the pKa in the reaction (H+) + (A-)→HA, which statement is correct?

<p>C</p> Signup and view all the answers

When the pH is less than the pKa in the reaction (H+) + (A)→(HA+), which statement is correct?

<p>F</p> Signup and view all the answers

What is the pH of a 1 liter solution where you mixed lactic acid and NaOH so that the final concentrations are 0.35 M lactic acid and 0.15 M sodium hydroxide?

<p>3.78</p> Signup and view all the answers

Which atom/functional group ionizes in one of the functional groups on this molecule?

<p>E</p> Signup and view all the answers

At what approximate pH does this molecule ionize?

<p>2-5</p> Signup and view all the answers

Assuming that the R group does not ionize, what is the net charge on this amino acid at pH = 7?

<p>0: both the amino and carboxyl are ionized at pH = 7 (A)</p> Signup and view all the answers

Which acid (and its conjugate base) would be the best buffer at pH = 3.7?

<p>Acid C (D)</p> Signup and view all the answers

The hydrogen bonds that cause the formation of an alpha helix occur mainly between which components?

<p>Alpha carbon of one amino acid and the carbonyl of another amino acid (B)</p> Signup and view all the answers

Identify which of these synthetic polypeptides can form an alpha helix at the given pH values.

<p>Both A and B (D)</p> Signup and view all the answers

Which substitution would you choose for serine 146, given a goal of maintaining size/shape but changing properties?

<p>Alanine (A)</p> Signup and view all the answers

What type of amino acids are most likely to appear in the interior of a protein?

<p>Hydrophobic amino acids (D)</p> Signup and view all the answers

A word that describes a protein that is in a dysfunctional state is?

<p>Denatured (C)</p> Signup and view all the answers

Which of the following is a better statement of Levinthal's paradox?

<p>Statement B (D)</p> Signup and view all the answers

Which types of interactions are primarily responsible for maintaining protein secondary structures?

<p>Hydrogen bonds (D)</p> Signup and view all the answers

What does it mean for a protein to be in the 'native conformation'?

<p>It is in the lowest energy conformation (C)</p> Signup and view all the answers

The pH of a black coffee is ~5, while the pH of lemon juice is ~2. Lemon juice has?

<p>1000 times higher [H+] than coffee (D)</p> Signup and view all the answers

Which of the following is the most accurate and comprehensive definition of chiral isomers?

<p>Definition A (C)</p> Signup and view all the answers

Design a coiled-coil protein for a nanotechnological application. What amino acid will you put at position d/d'?

<p>Alanine</p> Signup and view all the answers

What amino acid will you put at position a/a' in the coiled-coil protein design?

<p>Leucine</p> Signup and view all the answers

What amino acid will you put at position e/e' in the coiled-coil protein design?

<p>Lysine</p> Signup and view all the answers

What amino acid will you put at position f/f' in the coiled-coil protein design?

<p>Serine</p> Signup and view all the answers

How many equivalents of NaOH will it take to completely titrate phosphoric acid?

<p>3</p> Signup and view all the answers

At pH = 14, which of the molecular species above is predominant?

<p>D</p> Signup and view all the answers

At pH = 6, which of the molecular species above is predominant?

<p>B</p> Signup and view all the answers

What secondary structure primarily composes the oxygen-binding protein myoglobin?

<p>Alpha Helix (D)</p> Signup and view all the answers

The impression of open space in myoglobin is likely correct.

<p>False (B)</p> Signup and view all the answers

Which of the tri-peptides above is most likely to be found as part of a transmembrane alpha helix?

<p>Tri-peptide A (A)</p> Signup and view all the answers

Which of the tri-peptides above is most likely to be phosphorylated?

<p>Tri-peptide C (D)</p> Signup and view all the answers

For option E, what will be the total charge for the tri-peptide at pH 1?

<p>+2</p> Signup and view all the answers

Flashcards

Amphipathic

Molecules that have both a hydrophilic (water-loving) region and a hydrophobic (water-hating) region.

Hydrophilic

Molecules attracted to water, often polar or charged.

Hydrophobic

Molecules that repel water and don't interact well with aqueous environments. Often non-polar.

pH

A measure of the acidity or alkalinity of a solution. Lower pH means more acidic.

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Lactic Acid

A weak acid with a pKa of approximately 3.9.

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Sodium Hydroxide (NaOH)

A strong base, often used in chemical reactions.

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Isoleucine

A specific amino acid with branched side chain. Essential for protein synthesis.

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Peptide bond

A covalent bond between the carboxyl group of one amino acid and the amino group of another.

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Alpha helix

A specific type of secondary structure in proteins, characterized by a helical shape.

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Hydrogen Bonding

A type of chemical bond that involves the interaction between a hydrogen atom and an electronegative atom. Important for protein stability and interactions.

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Native Conformation

The functional, three-dimensional structure of a protein.

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Denaturation

Loss of a protein's native conformation, resulting in loss of function.

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Coiled-coil protein

A type of protein structure that is characterized by its elongated shape.

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Tri-peptide

A small protein composed of three amino acid residues.

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Post-translational Modification

A process that occurs after a protein has been synthesized, modifying its structure or function.

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Charge Calculation

The process of determining the net charge of a molecule at a particular pH.

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Isoelectric Point (pI)

The pH at which a molecule is electrically neutral.

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Full Ionization

A state where a molecule has lost all its electrons or gained a full number of electrons.

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Acidity (pKa)

A measure of a molecule's ability to donate or accept protons.

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Hydrophilic Amino Acids

Amino acids with side chains that are attracted to water.

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Hydrophobic Amino Acids

Amino acids with side chains that are repelled by water.

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Polar Uncharged Amino Acids

Amino acids that have a polar uncharged side chain.

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Charged Amino Acids

Amino acids that have a charged side chain.

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Positions a/a', d/d', g/g'

Positions in a coiled-coil protein helix, defined by their relative orientation.

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Base

A molecule that can accept a proton (H+).

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Acid

A molecule that can donate a proton (H+).

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Logarithmic Scale

A pH scale where each unit represents a tenfold change in hydrogen ion concentration.

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Titration

The process of changing the pH of a solution.

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Equivalence Point

The point in a titration where the solution is neither acidic nor basic.

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Partial Ionization

A state where a molecule is not fully ionized.

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Study Notes

Key Terms and Definitions

  • Amphipathic: Molecules that possess both hydrophobic and hydrophilic regions, influencing their behavior in solution.
  • Hydrophilic: Molecules that interact favorably with water, often polar or charged.
  • Hydrophobic: Molecules that repel water and do not interact well with aqueous environments.

pH and Solutions

  • pH of Sulfuric Acid: 1x(10^-9) M sulfuric acid approximates a pH slightly below 7, indicating a dilute acidic solution.
  • pH of Lactic Acid and NaOH Mixture: A solution containing 0.35 M lactic acid (pKa = 3.9) and 0.15 M sodium hydroxide yields a pH of approximately 3.78.

Amino Acids and Titration

  • Amino acid isoleucine undergoes full titration represented by a specific curve shape, typically exhibiting sigmoidal properties.
  • Peptide bonds, represented by letter C, connect amino acid residues, while certain bonds do not freely rotate.

Hydrogen Bonding and Molecular Structure

  • No hydrogens from the specified molecule can engage in hydrogen bonding if it's saturated or lacks donor/acceptor sites.
  • Molecular structures such as alpha helices are stabilized primarily by hydrogen bonds between backbone atoms, not R-group interactions.

Protein Structure and Properties

  • Specific amino acids, like serine, arginine, and their substitutions impact protein interactions and structural integrity.
  • Hydrophobic amino acids are typically found in the interior of proteins, contributing to stability.
  • Denatured proteins are dysfunctional, losing their native conformation, which is their lowest energy and functional state.

Acid-Base Chemistry

  • Lemon juice (pH ~2) has approximately 1000 times higher hydrogen ion concentration than black coffee (pH ~5), illustrating the logarithmic nature of pH scale.
  • The net charge of amino acids at pH 7 can vary depending on their functional groups' ionization states.

Synthesis and Coiled-Coil Proteins

  • Design of coiled-coil proteins requires careful selection of amino acids that fulfill specific roles while considering their properties under varying pH conditions.
  • Specific positions in the coiled-coil helix (designated a/a', d/d', g/g') determine the overall structure and functionality based on chosen amino acids.

Tri-Peptides and Protein Structure

  • Characteristics of tri-peptides vary based on amino acid composition, influencing their likelihood to reside in transmembrane regions or to undergo post-translational modifications like phosphorylation and disulfide bond formation.

Charge Considerations

  • Charge calculations for peptides at specific pH levels are crucial for understanding their behavior in biological systems, with implications for protein interactions and stability.

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Test your understanding of key concepts in biochemistry with this Exam 1 flashcard quiz. Each card challenges you to classify molecules as hydrophobic, hydrophilic, or amphipathic. Perfect for students preparing for their biochemistry exams.

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