BMSC 200 Midterm 1

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100 Terms

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Definition of Biochem

Study of life at a molecular level and the application of the principles of chemistry to explain biology

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What are the 4 Major classes of biomolecules?

1. Proteins

2. Nucleic Acids

3. Lipids

4. Carbohydrates

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Does the considerable difference in all living life mean they are different molecularly?

All organisms are remarkably uniform at a molecular level

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What do all organisms use?

Common building blocks to create common biomolecules (nucleic acids, proteins, polysaccharides, and lipids)

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4 Different Foundations of Life

1. Chemical

2. Energy

3. Genetic

4. Evolutionary

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What are the four main elements that compose around 98% of most organisms?

Carbon

Oxygen

Hydrogen

Nitrogen

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What are all known life forms based from?

Carbon

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How many people could naturally occuring nitrogen in the world feed?

4 Billion

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Who was able to get "bread from air" using nitrogen from the air as fertilizer

Fritz Haber

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How much is a human worth?

-Chemically only less than a dollar

-Looking at the chemical components like tissues, organs, and biomolecules have an estimated value of $45 000 000

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What is the next best candidate as the chemical foundation of life?

Silicon

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Why does Carbon work better than Silicon?

-C-C bonds are stronger than S-S bonds

-C-C bonds release more energy on combustion than S-S bonds

-Combustion of C-C bonds are soluble and remain active in biosphere

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What do functional groups determine?

The collective properties of functional groups determine the structure, function, and propeties of the biomolecule

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What does understanding the structure-function relationship of biomolecules help predict?

Molecular function, complex biology, and rational development of treatments

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Conformation

Flexible spatial arrangment of atoms within a molecule (changeable without breaking bonds)

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Configuration

Fixed spatial arrangement of atoms with a molecule (Not changeable unless covalent bond is broken)

-Conferredby either double bonds or chiral centers

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Geometric Isomers

(Cis-trans) Same chemical formula but different configuration of groups attached to a non-rotating double bond

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Cis

Same side of double bond

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Trans

Opposite side of double bond

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Chiral Carbon

4 different substituents attach to a single carbon that can be arranged differently in space creating 2 stereoisomers

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Construction

Biomolecules are often constructed from one stereoisomer

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Interactions

Interactions between biomolecules, as well as between biomolecules and small molecules, are stereospecific

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Simplicity

Simple, conserved reactions for synthesis and degradation

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What do chemical synthesis of molecules with asymmettric carbons create?

A mixture of all chiral forms

-Each form can have different effects

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4 Major Classes of Biomolecules

1. Protein

2. Carbohydrates

3. Nucleic Acids

4. Lipids

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The Case of Thalidomide

Ex. chemical synthesis of molecules created a different mix of chiral forms

-One helped with nausea and the other caused birth defects

-Dr. Francis Kelsey a reviewer from the FDA denied the drug

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3 Biological Polymers

1. Simplicity- Simple, conserved reactions for synthesis and degration

2. Recycling-Biomolecules can be digested back to component building blocks which are reusable

3. Diversity- Molecules of incredible complexity can be generated

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Proteins

-Linear polymers of aminoacids

-20 different amino acids

-Amino acids link into chains that create complex patterns with distinctly different purposes (proteins)

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Polysaccharides

-Carbohydrate

-Monosaccharides that are linked together to form a polymer

-Serve biological roles like structure, energy storage, and cellular recognition

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Nucleic Acids

-Linear polymers of nucleotide building blocks

-5 "building blocks"

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Lipids

Lipids are aggregates of "building blocks"

-Serve in energy storage, formation of membranes, and signalling

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Prokaryotes

-Small single cell organism

-Growth is rapid allowing quick adaptation

-Single compartment , the nucleoid

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Eukaryotes

Large complex cells

-Make up multi-cellular organisms

-Contain organelles

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Around how many prokaryotic and eukaryotic cells are in your body?

30 trillion eukaryotic cells and 100 trillion prokaryotic cells

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What does bacteria in the gut do?

Bacteria in the gut helps digest foo and maintain a functional immune system

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What does Microflora in the gut do?

Impacts health

-Depression, anxiety, obesity, and intelligence

"some people are calling the gut the second brain" - Scott Napper

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Are bacteria friends?

Yes, bacteria are my friends

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Vitro

Studies the behaviour of molecules outside the context of the cell and or organism (in glass)

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Vivo

Studies that occur within the cell or organism (in the living)

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First Law of Thermodynamics

Energy can be transferred and transformed, but it cannot be created or destroyed.

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Second Law of Thermodynamics

Nature has a tendency toward greater total entropy of the universe as it continually increases

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Gibbs Free Energy Theory

Energy changes during chemical reactions

-Free energy can be defind in terms of:

Enthalpy- # and kinds of bonds Entropy- Degree of randomness Temperature-In Kelvin

G = H - TS

G > 0 = endergonic

G < 0 = exergonic (spontaneous)

G = 0 = equilibrium

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Enthalpy (H)

Reflects the number and kinds of bonds

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Entropy (S)

The degree of randomness

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Temperature

Degrees Kelvin

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Energy Coupling

Cells thermodynamically drive unfavourable ractions by couply endergonic(energy requiring) and exergonic reactions (energy releasing)

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ATP in Metabolism

-Serves as an energy currency

-ATP serves as the link between catabolic reactions and anabolic reactions

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Steps of Replication

1. DNA undergoes transcription

2. RNA undergoes translation

3. Results in a protein

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Nucleotide Sequence

Dictates the sequence of amino acids added into a protein

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What does amino acid sequence do?

Dictates proteins structure

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Water

-Abundant molecule in living organisms

-Both passive and active roles

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Passive Role of Water

Structure of biomolecules forms in response to interactions with water

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Active Role of Water

Water is a participant in many biochemical reactions

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What gives water a permanent dipole?

Oxygen is more electronegative than hydrogen

-Forms electrostatic interactions

-Forms hydrogen bonds

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What can random changes in genotypes do?

Can change the phenotype that can lead to an advantage or disadvantage for the organism

(Evolution)

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What is the basic unit of DNA?

Two complimentary strands

-Each strand is a linear polymer of 4 types of building blocks

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What is the most abundant molecule in living organisms?

Water

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Passive Water Molecule

Structure of biomolecules forms in response to interaction with water

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Active Water Molecule

Water is a participant in biochemical reactions

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Alternate liquids that could support life

Ammonia and Formamide

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What does the dipole of a water molecule influence?

-Forms electrostatic interactions with charged molecules

-Forms hydrogen bonds

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What can both Oxygens and nitrogens serve as?

Hydrogen bond donors and acceptors

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How strong is a hydrogen bond relative to a covalent bond?

5% the strength of a covalent bond

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What does the strength of a hydrogen bond depend on?

its geometry

-anti-parallel beta sheets more stable than parallel

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How many hydrogen bonds can a water molecule form?

4- 2 as a donor and 2 as an acceptor

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In water water is the average hydrogen bond per molecule?

3.4 "flickering cluster"

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What can influence the properties of water?

Great internal cohesion between water molecules and hydrogen bonds

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Heat Vaporization

The amount of heat required to vaporize a liquid at its boiling point

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Specific Heat Capacity

The amount of heat required to raise the temp of a substance by one degree

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Unusual Properties of Water

When in solid form the arrangement of ice has a lower density than liquid water making ice float

-Water has a higher melting, and boiling point

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Polywater

Form of water with higher boiling point, lower freezing point, and higher viscosity

-Fear it could be weaponized

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Electrostatic Interactions

Molecules interact with charged solutes through formation of payers of hydration

-Small size and permanent dipole makes water great in interacting both positively and negatively charged ions

-Water shields charged groups and diminishes strength

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Molecule Solubility in water

Hydrophilic = molecules polar

Hydrophobic = molecules non-polar

Amphipathic = both hydrophobic and hydrophilic portions (most molecules)

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What do non-covalent interactions enable?

-Transient, dynamic interactions

-Flexibility, formation of structure and function

-Binding of reactants to enzymes

-Recognition between molecules

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Non-covalent Interactions Include

1. Hydrogen bonds

2. Ionic interactions

3. Hydrophobic interactions

4. Van Der Waals interactions

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What are Hydrogen bonds critical for?

Specificity of biomolecular interactions not for the formation of biomulecular structures

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Van Der Waals Forces

Interaction between permanent and induced dipoles (short range, low magnitude interactions

-When two surfaces come together a large # of atoms are brought into VDW contact

-Abundant in the core of folded proteins

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Hydrophobic Effect

Drive to have polar groups interactin with water and non-polar regions shielded away from it

-Proteins fold to make this happen

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What does the folding of a polypeptide do?

Decreases entropy of polypeptide but increases the entropy of the associated water

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What is the ion product of water?

Kw

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ph = ?

the difference of 1 pH unit equals a 10-fold difference in H+

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Which acids and bases dissociate completely in water?

Strong acids and bases

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Amphipathic Molecules

Hydrophilic regions interact with water but hydrophobic regions cluster together presenting the smallest surface to water

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Which acids and bases do not dissociate completely in water?

Weak acids and bases

-Dissociation can be quantified

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pKa =?

-log Ka

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What happens when pH = pKa

Solution is best able to resist changes in pH

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Stronge acid = ____pKa

Low

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Peptide bonds

Covalent linkages between carboxyl group of one AA and amino group of another

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How do peptide bonds form?

Condensationg reaction involving generation of a water molecule

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Repeating pattern of Polypeptide main chain

NCCNCC

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Primary Structure

Linear sequence of Amino Acids

-Info for specifying correct folding contained here

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Secondary Structure

Localized interactions within a polypeptide

-Maintained by hydrogen bonds between main chain amide and carbonyl groups

-Peptide bond has both hydrogen bond acceptors and donors

-Is favoured

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Tertiary Structure

Final folding pattern of a single polypeptide

-Amino Acid sequence determines tertiary structure

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Quaternary Structure

Folding pattern when multiple polypeptides are involved

-Help facilitate unique dynamic combinations of structure/function

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Amino Acids

The building blocks of proteins

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Phi and Psi

Can range from -180 to 180

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Simplicity of Chemistry

One reaction for polymerization the other for degradation

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Recycling

Biomolecules can be digested into reusable building blocks

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Henserson-Hasselbalch Equation

1. Relationship of the pH of the solution

2. The pKa of the weak acid

3. Relative concentrations of the weak acid and conjugate base

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Diversity

Potential for vast # of molecules of different lengths and sequences