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THE U / Biology / BIOL 1610 / What is the change in heritable characteristics over successive genera

What is the change in heritable characteristics over successive genera

What is the change in heritable characteristics over successive genera

Description

School: University of Utah
Department: Biology
Course: Fundamentals of Biology
Professor: Lucas moyer-horner
Term: Fall 2019
Tags: Biology, Macromolecules, Proteins, Enzymes, nucleic, acids, polymers, carbon, nucleotides, and amino acids
Cost: 50
Name: Exam 1 Study Guide
Description: Covers key concepts from classes to study.
Uploaded: 09/19/2019
9 Pages 54 Views 9 Unlocks
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CLASS 2: WHAT IS LIFE 


What is the change in heritable characteristics over successive generations?



Biology is the study of how LIFE works! 

Properties of life: 

1. Membrane delimited

a. Semi-permeable membrane

2. Stores and follows instructions

a. Nucleic acids

3. Stores energy, uses energy

a. Sunlight, organic compounds (sugars, lipids, proteins) & inorganic compounds (hydrogen, sulfide, nitrate) converts to ATP

4. Self replicating

5. Evolving

a. Change in heritable characteristics over successive generations

6. Controls its functions and responds to the environment

a. Proteins

- These properties of life are facilitated by biomolecules!


What is the fast replicating type of cell?



- The smallest unit that meets all these properties is a CELL!

Types of Cells: 

- Prokaryotic Cells (Archaea & Bacteria)

- Unicellular, no nucleus, small, no membrane bound organelles, fast replicating - Eukaryotic Cells (Protozoa, Fungi, Plant, Animals)

- Both unicellular & multicellular, nucleus & membrane bound organelles, larger Fundamental Concept: Life’s properties are facilitated by biomolecules! 

CLASS 3: CHEMISTRY OF LIFE 

All matter is composed of elements! Elements are made up of atoms! 

Atoms:

- Electrons in valence shell determine chemical behavior

- Inner shell holds up to 2 electrons, second shell holds up to 8


What is osmosis?



We also discuss several other topics like Who created a simple microscope with a lens and focus knob?

- Atoms want full sets of electrons in each shell

Science involves repeating experiments, critically analyzing data, critiquing, & refuting inferences.

Types of Interactions: 

- 2 atoms with incomplete valence shells interact by sharing, donating, or receiving electrons so both complete valence shells aka CHEMICAL BONDS Covalent bond: sharing electrons Don't forget about the age old question of Who created an intervention for externalizing behaviour of adhd?

a. H, 1 bond

b. O, 2 bonds

c. N, 3 bonds

d. C, 4 bonds

e. P, 3 or 5 bonds (Phosphate is important molecule in bio)

Polarity is determined by the way electrons are shared →

- Polar Covalent Bond: Unequal sharing electrons Don't forget about the age old question of What is the importance of "circular flow diagram"?

- 2 bonded atoms have charge difference

- Non-Polar Covalent Bond: Equal sharing 

- 2 bonded atoms have no charge difference

- More Electronegativity = Atoms attract electrons more 

Ionic Bond: A bond between oppositely charged “ions” 

- Transfer (no sharing) of electrons & big charge differences We also discuss several other topics like What is fast mapping?

Determining type of bond: Difference in electronegativity 

- 0-0.5 Non-Polar

- 0.5-1.7 Polar

- 1.7+ Ionic

Fundamental Concepts: 

- Atoms interact via bonds to form molecules

- Bonds are important for structure/function of biomolecules

- Biomolecules have polarity due to differences in electronegativity - Chemical properties of biomolecules determine functions

CLASS 4: WATER

Water molecules are: 

- Polar - because of differences in electronegativities

- Non bonded valence electrons of oxygen cluster on one end & push hydrogen atoms away

- Charged - forms Hydrogen bonds with other water/polar molecules

Hydrogen Bonds: If you want to learn more check out What are the three functions of today’s families?

- Weaker than covalent bonds, but numerous

- Happen between O-H, N-H, F-H

- H-bonds hold 2 strands of DNA double helix together (between bases) - Folding of protein structure relies on H-bonds & ionic bonds

- Protein structure important for function

Water is life’s solvent: 

- Polar molecules are hydrophilic (water-loving)

- Soluble: polar molecules that dissolve in water

- Water is solvent for most bio reactions

- Salt dissolves in water (salt is polar)

- Normal cell environment has balanced concentration of sodium inside & outside cell

- Hyponatremia: imbalance of more water (less salt) outside cell

- Movement of water into cell causes it to swell & burst

Osmosis: Water molecules pass through semipermeable membrane from less solute to more solute to equalize the concentration on each side of membrane

Fundamental Concepts: Water Chemistry 

- Essential for life

- Polar molecule

- Solvent of life

- Drives protein/dna structure If you want to learn more check out What are the six rules of critical thinking?

- Drives chemical reactions

CLASS 5: PH 

Water Ionizes: H2O to OH- & H+

PH:

- pH is the concentration of H+ 

- pH scale is logarithmic (0-14) 

- pH = -log10[H+]

- Difference of one unit represents 10-fold change in H+ concentration - pH of water is neutral = 7 (0.0000007 M)

- pH determines direction reaction goes → or ←

Acids: Molecules that donate H+ ions & decrease pH 

- pH is high with low H+ ion concentration (7-14)

Bases: Molecules that accept H+ ions & increase pH 

- pH is low with high H+ ion concentration (0-7)

Fundamental Concept: pH is a water dependant phenomenon that affects the activity of many biomolecules

CLASS 6: CARBON POLYMERS AND NUCLEIC ACIDS 

Carbon is Life’s Chemical Backbone! 

- Molecular diversity based on carbon properties

- Most molecules are composed of carbon bound to other carbons or elements Organic Compounds: Carbon-based molecules with functional groups attached - Functional Groups: groups of atoms that participate in chemical reactions - Amino - basic, charged

- Carboxyl - acidic, charged

- Carbonyl/Ketone - polar

- Hydroxyl - polar, hydrophilic

- Phosphate - acidic, charged, hydrophilic

Carbon can… 

1. Bond to 4 other atoms

2. Branch in four directions

3. Bonds can rotate freely

4. Carbon atoms can link up to form…

a. Strait, branched chains, rings, or carbon double bonds

Hydrocarbons: Molecules made up only of Carbon and Hydrogen

- Important fuel source

Polymers: long chains of smaller subunits called monomers that

- Macromolecules (organic molecules) are polymers and there’s 4 types... 1. Carbohydrates

2. Lipids

3. Proteins (most abundant)

4. Nucleic Acids

Macromolecules:

- Made by dehydration synthesis (loses water molecule)

- Broken down by hydrolysis (gains water molecule)

- Both require enzymes

Nucleic Acids (DNA & RNA) Structure & Function:

- DNA stores the instructions for cellular work & is heritable 

Types of Nucleic Acids: 

- RNA is… 

- Single stranded, can fold back on self to form loops, can fold into 3D structure - DNA is… 

- Double stranded, helix, coil further with proteins into more compact structure Structure of Nucleic Acids: 

- Nucleotides - long polymers made by repeated subunits of monomers - Composed of: phosphate, sugar & nitrogen base

- DNA & RNA nucleotides have different sugar 

- DNA has deoxyribose sugar

- RNA has ribose sugar

- DNA & RNA have different bases 

- DNA has AGCT

- RNA has AGCU

Nucleotides also function as ATP in cell: 

- Bonds between phosphate groups can have high energy

Bases:

- Purines: A & G

- Pyrimidines: T, C, U

- Bases are complementary & H-bond with each other 

- A with T (& U): held together with 2 H-bonds

- A% = T% (or U%)

- G with C: held together with 3 H-bonds

- G% = C%

Nucleotide monomers join together via phosphodiester bonds to make nucleic acid: - Phosphodiester bonds: Link sugars in each chain

- 2 strands of chain are anti-parallel

Reading/Writing DNA: 

- 5’-AGCT-3’ 

- 5’ is phosphate group, 3’ is hydroxyl group

DNA structure allows replication: 

- 2 strands of parental duplex separate

- The bases are paired in the parental duplex

- Each parental strand serves as template for synthesis of new daughter strand using base pairing rules (A with T & G with C)

CLASS 7: PROTEINS STRUCTURE RELATES TO FUNCTIONS 

Proteins are involved in every cell function! 

- Most important role for proteins is as enzymes

- Protein structure is important for function

Enzyme: A type of protein that serves as catalyst (speed up and regulate chemical reactions) Antibody: defense proteins that bind pathogens & neutralize them or mark them to destroy Structure of Proteins:

a. Space filling model

b. Stick model

c. Ribbon model

Proteins are polymers of Amino Acids: 

- Aminos acid monomers are linked by peptide bonds to form a polypeptide via dehydration synthesis

Side chains (R group) determine the properties of amino acids and how they fold, they can be… - Hydrophobic/Hydrophilic

- basic/acid

Special Amino Acids: 

- Glycine - small easily tucks in

- Proline - linkage causes bends

- Cysteine - form S-S bonds

Primary Structure: linear chain/sequence of amino acids

Secondary Structure: results from interactions of nearby amino acids of the backbone - Alpha helix: carbonyl group forms H-bond with amide group 4 residues away - Beta sheet: adjacent strands that can run parallel or antiparallel, H-bonds form between

carbonyl groups in one polypeptide & amide group in a different polypeptide Tertiary Structure: 3D shape of polypeptide aka protein

- Formed by side chain (R group) interactions & bonds

Quaternary Structure: Multiple polypeptides/proteins/individual tertiary structures interacting

Protein Domain: part of protein sequence & tertiary structure that can evolve, function & exist independently of the rest of protein chain

Protein structure can be impacted by: 

- Denaturation: caused by changes in proteins environment

- Loses 3D shape and becomes inactive

- Heat & pH changes denature protein by impacting Hydrogen and ionic bonds - Mutation

Fundamental Concept: Proteins are structurally & functionally diverse. The structure of each protein is crucial for its function.

CLASS 8: ENZYMES 

Enzymes:

- Speed up chemical reactions

- Typically proteins (also RNA)

Chemical Reactions: break & form bonds

Hydrolysis via enzymes → Breaking of Covalent bonds 

Dehydration Synthesis via enzymes → Making of covalent bonds

Metabolism: sum total of all chemical reactions happening in bio system at given time - 2 types → 

1. Anabolic reactions: complex molecules are made from simple molecules; energy is required

2. Catabolic reactions: complex molecules are broken down to simpler ones; energy is released

- Most of these reactions require enzymes

How enzymes catalyze chemical reactions: 

1. Orientation: Enzymes hold substrates (reactants) so that the bonds that need to form are oriented favorably

2. Physical Strain: enzymes apply tension on substrates (reactants) so that bonds that need be broken are under strain

3. Chemical charge: enzymes provide special micro-environment that favors reaction Active Site: location on enzyme that substrate binds for chemical reaction to occur (break down or form into product)

Enzymes as Catalysts: 

- E + S ( → or ← ) ES ( → or ← ) E + P 

- E = Enzyme, S = Substrate (reactant), P = Product

- Enzymes are not used up

- Enzymes are not changed by the reaction

- Enzymes catalyze the same reaction repeatedly

Enzyme Regulation:

- Competitive Inhibition - Inhibitor can bind to active site of enzyme, competing with substrate & reducing speed of reaction

- Allosteric Regulation: effector binds to enzyme at site different than active site, changing its shape

- Active form: can bind substrate (enzyme activated)

- Inactive form: cannot bind substrate (enzyme inhibited)

- Allosteric Inhibitor leads to → no product formed 

- Allosteric Activator leads to → product formed 

- Biosynthetic Pathways: Series of enzymatic steps that build specific products

Rubisco: An important but sloppy enzyme

- Reaction rate is slower because it often binds with oxygen on accident, instead of CO2

Fundamental Concept: Enzymes promote chemical reactions through physical interaction with substrates. The rates of enzymatic reactions can vary depending on properties of enzyme, the concentration of substrate or by presence of inhibitors.

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