BIOC 460/660 Study Guide
21 Questions
1 Views

Choose a study mode

Play Quiz
Study Flashcards
Spaced Repetition
Chat to lesson

Podcast

Play an AI-generated podcast conversation about this lesson

Questions and Answers

What is the significance of the isoelectric point (pI) in amino acids?

  • It shows the hydrophobicity of the R-groups.
  • It indicates the pH at which the amino acid has no net charge. (correct)
  • It reveals the molecular weight of the amino acid.
  • It determines the solubility of amino acids in water.
  • Which of the following techniques would be most effective in separating proteins based on their size?

  • Affinity chromatography
  • Ion exchange chromatography
  • Size exclusion chromatography (correct)
  • Isoelectric focusing
  • What is a zwitterion in the context of amino acids?

  • It refers to an amino acid in a neutral state with both positive and negative charges. (correct)
  • It is another term for dipeptide formation.
  • It describes an amino acid that can only exist at high pH levels.
  • It indicates an amino acid with a single charge.
  • Which statement about peptide bond formation is true?

    <p>Peptide bonds are formed when an amino group reacts with a hydroxyl group.</p> Signup and view all the answers

    What property of proteins is primarily utilized in column chromatography for their separation?

    <p>Charge and binding affinity</p> Signup and view all the answers

    What defines the equilibrium constant in a chemical reaction?

    <p>The ratio of the concentration of products to reactants at equilibrium</p> Signup and view all the answers

    How does an increase in temperature generally affect reaction speed?

    <p>It increases the speed of the reaction due to higher kinetic energy</p> Signup and view all the answers

    What is a characteristic of water that makes it essential for life?

    <p>It has a high specific heat capacity</p> Signup and view all the answers

    What is the reason ice floats on water?

    <p>Ice is less dense due to its crystalline structure</p> Signup and view all the answers

    What does the Henderson-Hasselbalch equation relate?

    <p>pH, pKa, and the concentration of acids and bases</p> Signup and view all the answers

    Which of the following describes the hydrophobic effect?

    <p>The tendency of nonpolar substances to aggregate in aqueous solution</p> Signup and view all the answers

    What do weak acids and their conjugate bases do in a buffer solution?

    <p>Resist changes in pH by neutralizing added acids or bases</p> Signup and view all the answers

    What happens when water ionizes?

    <p>It creates equal concentrations of H+ and OH- ions</p> Signup and view all the answers

    What is one unique feature of living matter that distinguishes it from non-living matter?

    <p>Ability to reproduce and evolve</p> Signup and view all the answers

    Which statement best describes the role of RNA in the origins of life?

    <p>RNA is considered a crucial initial molecule due to its ability to catalyze reactions.</p> Signup and view all the answers

    In thermodynamics, what is the significance of Gibbs free energy?

    <p>It represents the energy available to do work in a system.</p> Signup and view all the answers

    How do endergonic reactions differ from exergonic reactions?

    <p>Endergonic reactions absorb energy while exergonic reactions release energy.</p> Signup and view all the answers

    What type of system do living organisms represent in thermodynamics?

    <p>Open systems</p> Signup and view all the answers

    Which of the following functional groups is characteristic of biological molecules?

    <p>Hydroxyl group</p> Signup and view all the answers

    What is the primary reason why carbon is considered unique and critical to biochemistry?

    <p>Carbon can establish long chains and rings with diverse bonding.</p> Signup and view all the answers

    What defines the difference between catabolism and anabolism?

    <p>Catabolism involves breaking down molecules; anabolism involves building up molecules.</p> Signup and view all the answers

    Study Notes

    Biochemistry of Life

    • Features of living matter include responsiveness, reproduction, growth, and metabolism.
    • Life is divided into three domains: Archaea, Bacteria, and Eukarya.
    • Basic cell structure consists of a membrane, cytoplasm, ribosomes, and genetic material.
    • Unique cellular components include peptidoglycan in bacteria and chloroplasts in plants.
    • Energy and carbon sources are crucial for cellular processes, with glucose being a primary input.
    • Essential elements for life: carbon, hydrogen, nitrogen, oxygen, phosphorus, and sulfur.
    • Carbon's tetravalence allows diverse bonding and compound formation.
    • Common functional groups include hydroxyl, carboxyl, amino, and phosphate.
    • Cis vs. trans configurations affect molecular shape and function.
    • The origin of life theory suggests simple molecules led to complex organic compounds.
    • RNA is postulated as the first genetic material due to its ability to store information and catalyze reactions.
    • Mutation contributes to the fidelity of information replication and genetic diversity.
    • Endosymbiotic theory explains the origin of organelles through symbiotic relationships.

    Thermodynamics

    • Living organisms adhere to the laws of thermodynamics, particularly energy conservation.
    • Energy transformation is fundamental for biological processes.
    • Equilibrium refers to a state of balance, while dynamic steady-state indicates constant change.
    • Living organisms are open systems, exchanging matter and energy with their environment.
    • Metabolism encompasses catabolism (energy-releasing) and anabolism (energy-consuming) processes.
    • Gibbs free energy indicates the maximum reversible work; essential for predicting reaction spontaneity.
    • Entropy, enthalpy, and temperature influence free-energy calculations.
    • Reaction spontaneity is distinct from reaction rate; endergonic reactions require energy, while exergonic reactions release it.
    • The equilibrium constant relates to standard free-energy changes, illustrating reaction balance.
    • Reaction coupling allows non-spontaneous reactions to occur by associating them with spontaneous ones.
    • Biological catalysts (enzymes) lower activation energy, enhancing reaction rates.

    Water

    • Water is vital for life due to its unique properties and solvent capabilities.
    • A water molecule is polar, enabling hydrogen bonds with other molecules.
    • Ice is less dense than liquid water due to hydrogen bonding creating a crystalline structure.
    • Water's solvent properties lead to interactions with both polar (hydrophilic) and nonpolar (hydrophobic) substances.
    • Amphipathic molecules possess both hydrophilic and hydrophobic properties, influencing membrane structure.
    • Noncovalent interactions, such as hydrogen bonds and Van der Waals forces, stabilize molecular structures.
    • Hydrophobic effects arise when nonpolar substances aggregate to minimize exposure to water.
    • Colligative properties, like boiling point elevation and freezing point depression, depend on solute concentration.
    • Osmotic pressure is the force generated by water movement across a semipermeable membrane, critical for cell function.

    Ionization of Water, Dissociation of Weak Acids, and Buffers

    • Ionization of water produces H+ and OH- ions; pure water maintains a neutral pH (~7).
    • Proton hopping refers to the rapid transfer of protons between water molecules.
    • The ion-product constant (Kw) aids in calculating pH; pH measures hydrogen ion concentration.
    • Strong acids fully dissociate in solution; weak acids only partially dissociate.
    • Acid dissociation constant (Ka) quantifies weak acid strength, while pKa is its logarithmic form.
    • Buffers resist changes in pH by neutralizing added acids or bases, vital for biological systems.
    • Henderson-Hasselbalch equation relates pH, pKa, and the ratio of concentrations of acid/base pairs.

    Amino Acids, Peptides, and Proteins

    • Amino acids consist of an amino group, a carboxyl group, and a variable R-group.
    • There are 20 standard amino acids, each with distinct structures and properties.
    • Stereoisomer configuration is crucial for protein function; L and D forms exist.
    • Amino acids are classified based on R-group characteristics: polar, nonpolar, basic, and acidic.
    • Zwitterions are dipolar ions that form at specific pH points, influencing solubility and reactivity.
    • Isoelectric point (pI) indicates the pH at which the amino acid carries no net charge; affects mobility in electrophoresis.
    • Peptide bonds form between amino acids, releasing water through a condensation reaction.
    • Peptides can perform various biological functions, including signaling and catalysis.

    Protein Purification and Analysis

    • Protein properties such as size, charge, and affinity facilitate separation techniques.
    • Column chromatography separates proteins based on size or charge.
    • Ion exchange chromatography uses charged resin to attract oppositely charged proteins.
    • Size exclusion chromatography discriminates proteins by size during passage through porous media.
    • Electrophoresis applies an electric field to separate proteins by size and charge, including SDS-PAGE methods.
    • Isoelectric focusing separates proteins based on their isoelectric points.
    • 2D electrophoresis combines isoelectric focusing with SDS-PAGE for high-resolution protein analysis.
    • The specific activity of a protein indicates its enzymatic activity relative to its total amount.
    • Edman's degradation allows sequencing amino acids in proteins, while MALDI-MS gives mass data for analysis.

    Studying That Suits You

    Use AI to generate personalized quizzes and flashcards to suit your learning preferences.

    Quiz Team

    Description

    Prepare for your Foundations of Biochemistry and Molecular Biology I quiz with this comprehensive study guide. Focus on essential terminology and its application in lectures. Ensure you understand each term's definition and contextual usage for the course.

    More Like This

    DNA Flashcards
    9 questions

    DNA Flashcards

    RadiantLaplace9461 avatar
    RadiantLaplace9461
    Medical Terminology Flashcards
    17 questions
    Medical Terminology Quiz
    18 questions
    Use Quizgecko on...
    Browser
    Browser