Biochemistry of Life Processes

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Questions and Answers

What percentage of a human's mass is approximately carbon?

  • 18.5% (correct)
  • 25.0%
  • 12.5%
  • 30.0%

Which chemical element has the strongest tendency to attract electrons based on electronegativity?

  • Nitrogen
  • Carbon
  • Sulfur
  • Oxygen (correct)

Which type of bond involves the sharing of electron pairs between atoms?

  • Van der Waals interactions
  • Ionic bonds
  • Hydrogen bonds
  • Covalent bonds (correct)

What type of noncovalent interaction occurs between a charged group on one molecule and an oppositely charged group on another molecule?

<p>Ionic Interactions (D)</p> Signup and view all the answers

Which interaction is largely associated with the attraction of a partially positively charged hydrogen atom to a partially negatively charged atom?

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

Which arrangement minimizes electron pair repulsion in hydrogen bonding?

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

What element is least likely to have a significant role in forming biological compounds based on covalent bonding?

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

The stability of hydrogen bonds can be enhanced by which of the following factors?

<p>Linear atomic arrangement (C)</p> Signup and view all the answers

Which of the following interactions is weakest among noncovalent interactions?

<p>Van der Waals interactions (A)</p> Signup and view all the answers

What structural feature gives rise to resonance structures?

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

Which type of interaction is primarily responsible for the attractive forces between water molecules?

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

What characterizes Van der Waals interactions?

<p>They depend on temporary fluctuations in electron distribution. (B)</p> Signup and view all the answers

What happens to the pH when strong acids are added to a solution?

<p>pH decreases due to an increase in hydrogen ion concentration. (A)</p> Signup and view all the answers

Which of the following interactions involves the formation of water molecule 'cages'?

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

How can the concentration of an acid and its conjugate base be described when pH is equal to pKa?

<p>Concentrations of acid and conjugate base are equal. (A)</p> Signup and view all the answers

Which type of interaction is considered the weakest according to the strength hierarchy?

<p>Van der Waals interactions (B)</p> Signup and view all the answers

How would the dielectric constant of water be described?

<p>It is high, approximately 80. (D)</p> Signup and view all the answers

What effect does increasing hydrogen ion concentration have on pH?

<p>It lowers the pH. (D)</p> Signup and view all the answers

What separates a dipole within a molecule?

<p>Uneven distribution of electrons. (C)</p> Signup and view all the answers

What role do nonpolar molecules play in aqueous solutions?

<p>They are less favored compared to interactions among water molecules. (A)</p> Signup and view all the answers

What is indicated by a pH that is smaller than the pKa value of a weak acid?

<p>The concentration of the acid is greater than its conjugate base. (B), The concentration of the conjugate base is greater than the acid. (D)</p> Signup and view all the answers

Which statement about weak acids and weak bases functioning as buffers is true?

<p>They maintain a stable pH due to dynamic equilibrium. (C)</p> Signup and view all the answers

What occurs to bicarbonate concentration when carbon dioxide removal is increased during ventilation?

<p>Bicarbonate concentration decreases. (B)</p> Signup and view all the answers

Why do strong acids and bases form poor buffers?

<p>They dissociate completely, preventing stable pH. (A)</p> Signup and view all the answers

What is the primary function of a buffer system involving carbonic acid (H2CO3) and bicarbonate anion (HCO3-)?

<p>To maintain blood pH within a stable range. (D)</p> Signup and view all the answers

When considering buffer systems, what occurs if there is an excess of hydrogen ions (H+) in the solution?

<p>The buffer will release protons to stabilize pH. (D)</p> Signup and view all the answers

Which amino acid is represented as a diprotic acid with more than one dissociable hydrogen ion?

<p>Phosphoric acid (H3PO4) (A)</p> Signup and view all the answers

The dynamic equilibrium of a buffer system allows which of the following?

<p>Reversible reactions that maintain stable pH. (C)</p> Signup and view all the answers

What happens if the concentration of hydroxide ions (OH-) increases significantly in a buffered solution?

<p>The buffer neutralizes hydroxide ions to stabilize pH. (D)</p> Signup and view all the answers

How does hyperventilation affect the balance of bicarbonate in the blood?

<p>It decreases bicarbonate concentration through enhanced elimination. (C)</p> Signup and view all the answers

What is the primary role of the carbonic acid-bicarbonate buffer in the blood?

<p>To keep blood pH around 7.4 (A)</p> Signup and view all the answers

According to the Le Bel–Van 't Hoff rule, how many stereoisomers can a compound with 3 asymmetric carbon atoms have?

<p>8 (A)</p> Signup and view all the answers

Which statement correctly summarizes the concept of entropy in living systems?

<p>Entropy measures the randomness of molecules (B)</p> Signup and view all the answers

What stabilizes the tertiary structure of proteins?

<p>Hydrogen bonds and disulfide bridges (A)</p> Signup and view all the answers

Which of these statements is true regarding myoglobin?

<p>It supplies oxygen to muscle cells (B)</p> Signup and view all the answers

Which of the following describes the quaternary structure of proteins?

<p>Involves multiple binded polypeptide chains (D)</p> Signup and view all the answers

In the context of thermodynamics, what does enthalpy refer to?

<p>The heat content of a system during a process (C)</p> Signup and view all the answers

Which type of amino acids carries a positive charge?

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

What is the main factor that governs the stability of the carbonic acid-bicarbonate buffer system?

<p>The pKa value of carbonic acid (A)</p> Signup and view all the answers

Which of the following statements about isomers is correct?

<p>They are identical in molecular formula but differ in spatial arrangement (D)</p> Signup and view all the answers

Flashcards

Biochemistry

The study of chemical processes happening in living organisms.

Covalent Bond

A chemical bond formed by the sharing of electron pairs between atoms.

Resonance Structures

Different ways of representing the same molecule that differ only in electron distribution.

Electronegativity

The ability of an atom to attract electrons towards itself in a chemical bond.

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Hydrogen Bond

A weak attraction between a partially positive hydrogen atom and a more electronegative atom.

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Noncovalent Interactions

Attractive forces between molecules that are not covalent bonds.

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Ionic Interactions

Attraction between oppositely charged ions.

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van der Waals Interactions

Weak attraction between atoms due to temporary shifts in electron distribution.

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Biological Compounds

Compounds crucial for life, mostly carbon-based.

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Importance of Carbon

Carbon is essential to life, forming the backbone of many biological compounds.

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Van der Waals Interactions

Weak, attractive forces between molecules due to temporary fluctuations in electron distribution.

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Dipole

A molecule with a separation of charge, resulting in a positive and negative pole.

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Hydrogen Bonds

Strong attractive forces between a hydrogen atom covalently bonded to a highly electronegative atom (e.g., O, N) and another electronegative atom in a different molecule.

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Hydrophobic Interactions

Interactions between nonpolar molecules that are driven by the water molecules' tendency to associate with each other.

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Water as a Solvent

Water readily dissolves many substances, especially polar and charged compounds due to hydrogen bonding and ionic interactions.

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Water Cohesion

Water molecules interact strongly with each other due to hydrogen bonds.

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Acid

A proton (H+) donor.

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Base

Proton acceptor in a chemical reaction.

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pH

Measure of H+ concentration in a solution, ranging from 0 to 14.

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pKa

pH at which half of the acid is dissociated into its conjugate base.

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Titration curve

A graph that shows the change in pH of a solution as a titrant is added.

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pKa

The pH at which half of a weak acid is protonated (and half deprotonated).

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Weak Acid

An acid that does not fully dissociate in water.

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Buffer

A solution that resists changes in pH.

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Polyprotic Acid

An acid that can donate more than one proton (H+).

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Base

Proton acceptor.

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Bicarbonate in ventilation

Increased CO2 removal causes a decrease in acidity (alkalosis). Then bicarbonate shifts to restore blood pH

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Blood Buffer

Carbonic acid (H2CO3) and bicarbonate (HCO3-) in blood maintain pH between 7.35-7.45.

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Strong Acid/Base Buffering

Strong acids/bases do not make good buffers.

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Amino Acid

Organic compound possessing both amino and carboxyl functional groups.

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pH regulation in body

The human body maintains its pH between 7.2 and 7.5 using buffers like the carbonic acid-bicarbonate buffer, which keeps blood pH near 7.4.

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Carbonic acid-bicarbonate buffer

A buffer system in blood that helps maintain a stable pH.

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pKa of carbonic acid

The pH at which half of carbonic acid molecules are dissociated. It’s 6.1 in this case.

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Stereoisomers

Molecules with the same atomic connections but different spatial arrangements.

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Asymmetric carbon atoms

Carbon atoms bonded to four different groups.

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Le Bel–Van 't Hoff rule

The number of stereoisomers in a compound is 2^n, where n is the number of asymmetric carbon atoms.

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Protein composition and structure

Proteins are composed of amino acids, and their structure is defined by primary, secondary, tertiary, and quaternary forms, in which they have different bonds.

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Myoglobin

A protein that stores oxygen in muscle tissue, with a heme prosthetic group.

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Protein Structure (Tertiary)

The 3D arrangement of a polypeptide chain, stabilized by various interactions like hydrogen bonds and disulfide bonds.

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Protein Structure (Quaternary)

The arrangement of multiple polypeptide chains (subunits) in a protein complex, similar to tertiary structure in properties.

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Study Notes

Biochemistry of Life Processes

  • Life on Earth is carbon-based
  • 18.5% of human mass is carbon
  • Key elements in biological compounds: C, H, O, N, P, S

Covalent Bonds

  • Strongest bonds
  • Involve electron pair sharing between atoms

Electronegativity

  • Property describing an atom's electron attraction
  • Trend: O > N > S > C > P > H

Resonance Structures

  • Double bonds cause resonance structures
  • Not static bonds

Noncovalent Interactions

  • Ionic Interactions: Oppositely charged groups attract
  • Hydrogen Bonds: Partially positive hydrogen atoms attract partially negative acceptor atoms
  • 180° angle in hydrogen bonds minimizes electron pair repulsion, optimizes interaction and increases stability
  • Van der Waals Interactions: Weak, temporary attractive forces between molecules

Molecules in Aqueous Solutions

  • Interact with water through hydrogen bonding and ionic interactions
  • Water is a versatile solvent, especially for polar and charged compounds

Water (Hâ‚‚O)

  • Highly cohesive due to strong hydrogen bonding
  • High dielectric constant (80)

Acids and Bases

  • Acids: Proton donors
  • Bases: Proton acceptors
  • pH = -log[H+]
  • Buffers help maintain stable pH

Amino Acids

  • Peptide Bond Formation: Forms between amino acids
  • Hydrophobic Amino Acids: (e.g. Glycine, Alanine, Valine - hydrophobic, less attraction to water molecules)
  • Polar Amino Acids: (e.g. Serine, Threonine, Tyrosine - polar, more attraction to water molecules)
  • Positively charged: (e.g., Arginine, Histidine, Lysine)
  • Negatively charged: (e.g. Aspartate, Glutamate)

Stereoisomers

  • Different spatial arrangement of atoms
  • Le Bel-Van 't Hoff rule (2n)

Living Systems and Disorder

  • Entropy: Measure of disorder in a system
  • Enthalpy: Total heat content in a process
  • 2nd law of thermodynamics: Natural processes tend to increase disorder

Proteins

  • Primary Structure: Amino acid sequence
  • Secondary Structure: Hydrogen bonding patterns (alpha helix, beta sheet)
  • Tertiary Structure: 3D folding of a protein
  • Quaternary Structure: Multiple polypeptide chains

Myoglobin and Hemoglobin

  • Myoglobin: Heme protein for oxygen storage, single polypeptide chain
  • Hemoglobin: Heme protein for oxygen transport, 4 polypeptide chains (2 alpha, 2 beta)

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