• Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

Card Range To Study

through

image

Play button

image

Play button

image

Progress

1/249

Click to flip

Use LEFT and RIGHT arrow keys to navigate between flashcards;

Use UP and DOWN arrow keys to flip the card;

H to show hint;

A reads text to speech;

249 Cards in this Set

  • Front
  • Back

Biology

Science of life


Observation/ evidence based

Scientific method

Observe to generate a hypothesis


Make a prediction and test by experiments


Observations and experiments should be reproduceable

Null hypothesis

No affect

Alternative hypothesis

There is an effect

If null hypothesis is true

Accept null hypothesis and reject alternative

Test group

Conditions where test variable is changed

Control group

Know the result


Point of comparison

P value

0.05 error rate

The cell

Most basic unit of life

Prokaryotes structure

Nucleoid


Flagella


Cell wall


Capsule


Ribosomes

Eukaryotic cell

Mitochondria


Nucleus


Nucleolus


Cell membrane


Ribosomes

All cells

Have a cytoplasm


Cell membrane


Harness energy


Ribosomes


Store and transmit information for growth, function and reproduction (DNA)

DNA

Double stranded helix


Sequence of molecules that code cells information


Information can be copied from cell to cell or organism and progeny

Evolution

Change over time


Unity and diversity


Unity-common ancestor


Diversity- natural selection or artificial selection

Evolution example of moths

Light peppered moth easily seen on black bark


Dark pepper moth blends in so dark moth reproduces and survives

Artificial selection

Breed individuals with desired traits

a 99.9% bacterial cleaner does not always have the same effective amount

More resistant bacteria


Bacteria reproduce resistant bacteria

Phylogenic tree

Show relationship with ancestor and descendant


Closely related have more common traits

Atom

Makes up an element, this cannot be broken down further

118 elements known ? Natural? Artificial

94 natural


24 artificial

Elements essential to life

25



These atoms make up 94-96%of living matter

Carbon, hydrogen, oxygen and nitrogen

We have more oxygen because

It's heavier than hydrogen


We are made of 70% water

Trace elements

Required in minute quantities

Atoms structure and location

Protons positive


Electrons negative


Neutrons no charge


Protons and neutrons in nucleus


Electrons around nucleus

Atomic number

Number of protons


A specific element

Atomic mass

Protons + neutrons

Isotopes

Different neutrons for same element

Ion example sodium chloride

Sodium loses electron to be positive


Chloride gains electron to be negative

Horizontal row on periodic table

Same number of shells

Vertical column

Same number of electrons in outermost shell

Molecules

Atoms combine by chemical bonds

Ability of atoms to combine with other atoms

Determined by distribution of electrons in outermost shell

Chemical reaction

Reactants are transformed into products


Number of each atom remains the same


Arrangements differ

Covalent bond

Two atoms share valence electrons

How many covalent bonds can you have

Depends on amount of unpaired valence electrons

Double bonds

Atoms share two valence electrons

Molecule stability

Electrons fill the outermost shell (more stable)

Electronegativity

Atoms ability to attract electrons


O and n can attract electrons better than c and h

Non polar covalent bond

Atoms are shared equally

Polar covalent bond

One atom is more electronegative



the atoms do not share electrons equally resulting in partial charges

Polar covalent bonds in water

Oxygen pulls electrons closer to itself

Hydrogen bonds

Hydrogen is attracted to oxygen on the other water bond

Formaldehyde

is a polar molecule one end is partial positive, the other is partial negative


CH2O

Carbon dioxide

Non polar


Both ends are partial negative due to symmetry


Individual bond polarities cancel each other out


CO2

Nacl in water

oxygen is more electronegative than hydrogen so oxygen is partial negative and hydrogen is partial positive


Oxygen pulls na+ away and hydrogen pulls cl- away


Nacl is charged due to ionic bonds (see ionic bond)

Hydrogen bonds

Interactions between hydrogen. And more electronegative atom on another molecule


Hydrogen bonds are weaker than covalent bonds

DNA hydrogen bonds

In between the nitrogenous bases

Hydrophilic

Water loving


Ionic or polar

Hydrophobic

Afraid of water (non polar)

Cohesive behavior

Water molecules stick together with other polar molecules

Expansion upon freezing

Water is less dense solid

Ability to moderate temperature

Water resists temperature changes


In order to increase temperature hydrogen bonds must break

Versatility as a solvent

Water can dissolve more materials than any other liquid

Cohesion in plants

Adhesion to cell walls resists downward pull


Cohesion is Evaporation of water leaves pull water upwards from roots through water conducting cells

When water freezes

Forms a crystallin lattice structure with 4 other water molecules

Heat is released

Hydrogen bonds form

Heat is absorbed

Hydrogen bonds break

Sweating

Water molecules absorb heat and evaporate cooling us of

pH

Water exists as hydronium ion or hydrogen is. And hydroxide ion

pH formula

pH= -log(H+)

Basic

pH is above 7

Acidic

pH less than 7

Neutral

pH 7

Acid

Releases a H+

Base

Accepts H+ or releases OH-

pH scale is logarithmic

1 pH is a tenfold difference in H+ Concentration

Buffers

Minimizes changes in concentration of H+ and OH-


Weak acid base pairing that donates or accepts H+

Carbon

Organic molecules

Structure is associated with

Function

Carbon

Has four unpaired valence electrons


Methan four hydrogen connect producing a tetrahedron which rotates freely

Carbon atoms link to form

Branched or ring structure

Carbon double bonds

Share two pairs of electrons


Not free to rotate


Flat shape

Isomers

Spatial arrangement of atoms


Two molecules can have same chemical formula with different structure and function

Structural isomers

Differ in covalent bond arrangements

Cis trans isomers

Same covalent bond arrangements but differ in spatial arrangement due to double bonds


2 different groups

Enantiomers

Mirror image


Differs in shape due to chiral carbon


Chiral carbon is attached to four different atoms

Thalomide enantiomers

Mirror images


R effective against morning sickness


S causes birth and limb defect

Functional groups

Group of atoms attached to carbon skeleton


Involved in chemical reactions


Number and arrangement gives unique properties

Hydroxyl

-OH

Carbonyl

C double bonded to O

Carboxyl

Carbon bonded to hydroxyl and double bonded to O


Acidic when h leaves

Amino

NH2 accepts H becomes basic

Sulfhydrl

SH

Phosphate

Two double bonds to O and single bonds


Negative charge


H leaves making it basic

Methyl

CH3

Organic molecules

Proteins, nucleic acid, carbohydrates and lipids


Polymers consisting of monomers connected by covalent bonds

Proteins

Polymer of amino acids

Nucleic acids

Polymers of nucleotides

Polysaccharides

Polymers of monosaccharides

Lipids

Not a monomer

Limitless chemical diversity

Macromolecules from monomers

Proteins

Provide structural support and act as catalysts that facilitate chemical reactions


Diverse with tens of thousands of proteins


20 amino acid monomers

Structure of amino acid

Central carbon atoms


Carboxyl


Amino


Hydrogen


r group

Peptide bond

Amino acids joined together


Carbon to nitrogen through dehydration synthesis


Carbon loses OH and nitrogen loses H

Nucleic acids

DNA - genetic material


RNA- for protein synthesis

Nucleotide structure

Five carbon sugar


Nitrogenous base


One or more phosphate group

Bases

Adenine and guanine are purines


Thymine, cytosine and uracil are pyrimidines

Phosphodiester bonds

Phosphate is joined with sugar


Dehydration synthesis

Structure of DNA

Two strands of nucleotides twisted in a double helix sugar and phosphate form a backbone

Carbohydrates

One carbon two hydrogen one oxygen


Monosaccharide is one sugar


Disaccharide is two sugars


Polysaccharide is many sugars

Monosaccharides

Major energy source for cells


Raw material for building molecules


6 carbon sugar

Glycosidic bonds

Join monosaccharides

Starch

Storage polysaccharide by plants for energy


Made of alpha glucose below the plane of the ring

Cellulose

Structural polysaccharide and major component of wall of plant cells


Beta glucose above plane of the ring

Lactose intolerance

People stop producing lactase

Lipids

Hydrophobic


Not from monomers


E.g. fats phospholipids and steroids

Steroids

Testosterone and estrogen

Fats

Glycerol- three carbon alcohol with hydroxyl group attached to each carbon


Fatty acid long chain of carbons attached to carboxyl

Triacylglycerol

In Animal fat and plant oil


Structure- three fatty acids and glycerol


Attached by ester linkages


Mostly for storage

Saturated fatty acids

Max hydrogen atoms and no double bonds


Unsaturated fatty acids

Less than max hydrogen atoms and one or more double bonds

Van der waals forces

Constant movement of electrons lead to regions of slight charge


Charges attract or repel neighbouring molecules

DNA

Stores genetic information for protein


Plays role in transmission of information from parents to offspring to maintain identity overtime

Griffith experiment on genetic material step one

Two strains of bacteria one pathogenic and one harmless


He mixed killed virulent bacteria and living harmless of streptococcus pneumonia bacteria

Griffith experiment part two

Some living became pathogenic


Concluded that type of molecule in the debris contained genetic information for virulence

Transformation

Change in genotype and phenotype due to assimilation of foreign DNA

Griffith experiment part three

DNA transformed non virulent to virulent


Enzyme to kill DNA was unable to transform non virulent bacteria

Genome

Complete set of DNA

Genes

Specific stretch of DNA that codes for protein or RNA

Chromosome

In Prokaryotic is circular


In eukaryotic it is called chromatin


It consists of linear strands of DNA wrapped around histones forming a nucleosome

Histones

Protein

Replication

DNA copies itself almost exactly

Mutations

Most are harmful


Some are beneficial making organism better able to adapt

Nucleoside

Consists of sugar and base

DNA

Found by James Watson and Francis crick


Five carbon sugar, base and one or more phosphate groups

Phosphodiester bonds

Nucleotide sugar is linked with phosphate of neighbouring nucleotide


C-O-P-O-C linkages is a phosphodiester bond


Polarity of DNA

One end differs from the other phosphate negative so sugar is positive

DNA is read from

Five prime to three prime

Base pairing rules

Erwin chargraff


%A=%T


%C=%G

Rosalind franklin

Helical structure of DNA

DNA double helix structure

Two strands of DNA run in opposite directions


Sugar and phosphate outside


Bases inward


Purine binds with pyrimidine

Purine binds with pyrimidine

Through Hydrogen bonds

DNA is semi- conservative

Two strands of DNA unwind


Parental strand provides template for daughter strand

DNA copying

Quick and accurate


A dozen enzymes and proteins participate in DNA replication

Origin of replication

Two strands of DNA are separated


Opening up replication bubble


Replication proceeds in both directions until entire molecule is copies

DNA polymerase

Catalyzes DNA synthesis


Adds to three prime


Cannot make new strand

RNA primase

Synthesizes RNA primer

Lagging strand

Synthesizes away from replication fork

Leading strand

Synthesizes toward replication fork

Okazaki fragments

Discontinuous pieces of lagging strand

DNA polymerase

Removes RNA primer and replaces it with DNA


Proofreads it corrects an error by removing an incorrect nucleotide and inserts the correct one

DNA ligase

Joins DNA fragments together

Helicase

Unwinds DNA duplex at replication fork

Topoisomerase

Relieves stress from unwinding by breaking, partially unwinding and reattaching DNA strand

Single stranded binding proteins

Stabilize single strands of DNA

Lagging strand becomes shorter

RNA primer is removed and DNA remains unreplicated


Shortened template results in shorter chromosome


Pattern were to persist it would be severely shortened

Telomere

Consists of sequence TTAGGG repeated 1500 to 3000 times


Postpone erosion of genes

Adult somatic cells divide 50 times

Telomeres are shortened so cell stops dividing

Telomerase

Germ and stem cells have this


It prevents the chromosome ends from being shortened


Contains RNA template that restores original length of telomeres

Somatic cancer cells

Reactivate telomerase activity


So it keeps growing

Scientists can

Isolate identify and sequence DNA fragments


This can help determine risk factors, identify DNA at crime scene and produce genetically engineered organisms

Insulin

1. Human Gene insulin is amplified, cut and combined with bacterial DNA with a plasmid


2. Plasmid introduced into bacteria for protein production


3. Human insulin is isolated and purified from bacteria

Polymerase chain reaction

Amplifies specific DNA region


It needs a DNA template, DNA polymerase, primer and nucleotides

PCR

1.Template is longer than amplified region


2. 20 to 30 base primers used


3. Each round doubles number of molecules


4. 2n copies 2^30= 10^9

Gel electrophoresis

Electric current passed through


DNA moves to positive end


Smaller moves quicker

Restriction enzymes

Recognize and cleave specific sequences of DNA

Recombinant DNA

Recombines DNA from two or more different sources into a single molecule uses DNA ligase

Transformation

recombinant DNA introduced to bacterial cell


Bacteria are chemically induced to take DNA from outside cell


Bacterial cell divides and replicates


Replicating recombinant DNA

GMOs example

1. Sheep product human protein in milk for emphysema


2. Salmon increased hormone for rapid growth

DNA editing

1.CRISPR


2. Genomic DNA can be targeted specifically for cleavage by Cas9


3. Cut DNA is altered

RNA and transcription


RNA and transcription

RNA is used for DNA replication, transcription and translation RNA evolves and acts as a catalyst

DNA

DNA- double stranded


Hydrogen on sugar


A,T,C,G


Deoxyribonucleic sugar


Large in size


Monophosphate

RNA

Single stranded


A,U,C,G


Ribose sugar


Triphosphate


Smaller

Central dogma

1. Transcription rewrites DNA into RNA using same nucleotide language


2. Translation switches nucleotide language to amino acid language

% of human genome codes for protein

2%

Transcription

1. DNA unwinds one strand as template for RNA transcript


2. T is replaced with U


3. RNA polymerase changes it


It grows in five prime to three prime

Initiation and termination of transcription

Eukaryotic promoters contain sequence TATAAA


First nucleotide transcribed is 25 base pairs from TATA box

Eukaryotic promoter

Initiation requires general transcription factors binding to promoter


Transcription activator proteins bind to enhancer

Eukaryotic promoter

1.RNA polymerase binds to template DNA and unwinds it


2. Looping of transcriptional activator proteins, mediator complex, RNA Polymerase and general transcription factors are brought into close proximity for transcription to proceed

RNA polymerase two adds nucleotides to three prime end

1.Transcription occurs in RNA Polymerase complex


2.Two DNA strands separate and growing RNA strand forms duplex with DNA template

Polymerization reaction

1. Incoming nucleotides connect if they correctly pair


2. Three prime hydroxyl of growing strand attacks high energy phosphate bond of incoming riboucleotide providing energy to drive reaction


3. Two phosphates of incoming riboucleotide released as pyrophosphate

RNA primary transcript

RNA comes off DNA strand as primary transcript

Primary transcript

Contains information of gene transcribed and information needed to produce protein

mRNA

RNA molecule that combines with ribosome to direct protein synthesis

RNA processing

Primary transcript undergoes complex process of chemical modifications

Poly adenylation

The addition of 250 consecutive adenines to three prime end of mRNA


This helps export mRNA into cytoplasm


Protect end of transcript and stabilize RNA transcript

RNA processing

The addition of five prime cap consisting of seven methylguanosince

RNA processing

RNA splicing

Excision of introns


Leaves exons


90% of human genes contain at least one intron


Catalyzed by complex RNA and protein known as spliceosome

Alternative RNA splicing

One primary transcript codes for multiple genes


Gene formed depends on how transcript is spliced

Noncoding RNA

Ribosomal RNA found in ribosomes, the site of protein synthesis


Transfer RNA transports amino acids to site of protein synthesis

Amino acid

consists of an alpha carbon connected by covalent bonds to amino group, carboxyl group, hydrogen and R group

Bonds R groups of hydrophilic amino acids form

Hydrogen bonds

Basic and acidic amino acids

Hydrophilic

R groups Inside? Outside?

Hydrophobic inside


Hydrophilic outside

Primary structure (protein)

Amino acid sequence listed from amino end to carboxyl end


This structure determines secondary and tertiary structure


20^n is number of protein sequences

Secondary structure

Result of hydrogen bonding to backbone of polypeptide


Two types


Beta sheet


Alpha helix

Beta sheet

Pleated sheet that is stabilized by hydrogen bonds between carbonyl and amino group from one chain to the other

Alpha helix

A coil stabilized by hydrogen bonds between amino acid's carbonyl and amino group four residuals away

Tertiary structure

3D shape made of several secondary structures


Determined by spatial distribution of hydrophobic and hydrophilic groups along molecule and chemical bonds and interactions between R groups

Tertiary structure models

1.Ball and stick model- atoms in amino acid chain


2.Ribbon model emphasized alpha helices(twisted ribbon) and beta sheets (broad arrows)


3. Space filling model shows shape and contour of folded protein


Function of tertiary structure

Contours and distribution of charge outside molecule


Presence of cavities that might bind with smaller molecules inside

Function

Enzymatic proteins


Catalyze chemical reactions



Defensive proteins


Protect against disease


E.g. antibodies



Storage proteins


Storage of amino acids


E.g. ovalbumin



Transport proteins


Transport molecules from one place to another


E.g. channel proteins and hemoglobin

Functions two

Hormonal proteins


Messengers that regulate bodies activities



Receptor proteins


Helps cells communicate with external environment through use of signaling molecules



Contractile and motor proteins


Responsible for movement


E.g. actin and myosin



Structural proteins


Are fibrous and provide support

Denaturation of proteins

Alterations in pH, temperature and salt concentration causes protein to unfold and lose its shape and function


If optimal conditions return some proteins refold and regain functions

Quaternary structure

Many tertiary structures which influences shape and function of proteins


Subunits of quarternary structure can be identical or different

Collagen

Composed of three identical polypeptides coiled like a rope

Hemoglobin

Composed of four polypeptides, two copies of one type and two copies of a second type

Components of translation

mRNA, initiation factors, elongation factors, release factors, aminoacyl trna syntases, transfer RNA, ribosomal RNA and ribosomal proteins

Translation

Sequence of bases in mRNA specifies the order in which amino acids are added to synthesize a polypeptide

Ribosomes

Translation takes place


Coordinate functioning of mRNA and tRNA and synthesis of polypeptide

Ribosomes have two subunits

Small and large


Each subunit is composed of RNA and proteins


Large subunit contains three binding sites for tRNAs

Three binding sites on large ribosome subunit

Exit site


Peptidyl site


Aminoacyl site


Ribosome sequence

Continuous and non overlapping groups of three nucleotides


Constitute a codon


Reading frame is where ribosome begins reading sequence of nucleotides

tRNAs

Transfer RNA consists of a single RNA strand about 80 nucleotides long

tRNA

Picks up amino acid at three prime


Uses an anticodon to recognize codons in mRNA

Aminoacyl tRNA syntases

Connect amino acids to tRNA molecule


They are very accurate

tRNA

Base pairing

Specifies DNA, RNA and codon anticodon interactions

Codon and anticodon

Codon circled in black, anticodon circled in orange

Genetic code

20 amino acids specified by 64 codons

Redundant

Many amino acids specified by more than one codon

Unambiguous

One codon codes for one amino acid

Redundant

Wobble effect


mRNA can be translated with fewer than 64 tRNAs that would be required without wobble

Genetic code is nearly universal

Genes from humans can be cloned into other species and will identify the same polypeptide


Useful in biotechnology and genetic engineering

Process of translation

Step one Initiation


Initiator AUG codon is recognized and Met is established as first amino acid in new polypeptide chain



Elongation successive amino acids added to carboxyl end



Termination the addition of amino acids stops and polypeptide chain is released from the ribosome

Initiation

1. Initiation factors bind to five prime cap of mRNA


2.Initiation factors bring up tRNA met


3. Small subunit of ribosome is recruited


4. Complex scans for AUG codon


Initiation

Large ribosomal subunit joins complex


Initiation factors are released


Next tRNA is ready to join ribosome

Initiation

New tRNA is in place, Met detaches from tRNA and attaches by a peptide bond to the next amino acid

Initiation

Ribosome shifts one codon to the right removing uncharged tRNA to E site and the other tRNA to P site freeing the A site for next charged tRNA in line to come in

Elongation

Process continues in which successive amino acids are added one by one to the growing chain

Termination

Process occurs until stop codon


A release factors binds to A site causing the bond connecting to the polypeptide of tRNA to break this terminating translation

Mutations

Change in sequence of genetic material

Mutagens

Chemical increases probability of mutations

Mistake in transcription/translation that is not critical

Change of one protein

RNA is not heritable

Only heritable in viruses

Mutation rates

Mutation is rare for individual nucleotides

Highest rate of mutations

RNA viruses and retroviruses

Mutations in DNA replication occur in humans

One nucleotide in every ten billion

Mutations affect proteins

Affect level and timing of expression

Mismatch repair enzymes

Fix any error missed by DNA polymerases

Mismatch repair enzymes recognize parental strand from daughter strand

DNA methylation


New DNA is not modified yet

Types of Mutations

Nucleotide substitution


Frameshift mutation


Large scale (chromosomal mutations)

Nucleotide substitution is the most frequent

DNA is mismatched e.g. T is matched with G


In the next replication the nucleotide is correctly matched in the daughter strand e.g. G is matched with C

Point mutations

Depends on part of genome where mutation occurs


Coming or no coding region

Synonymous mutation

Does not change amino acid

Non synonymous mutation

Changes amino acid

Nonsense mutation

Changes amino acid to stop codon that terminates translation early resulting in incomplete polypeptide

Sickle cell disease

Inherited blood disorder from single nucleotide substitution in protein hemoglobin subunit beta globin



Non synonymous mutation


Oxygen carrying capacity is reduced


Molecules crystallize into a fiber

Frameshift mutation

Insertion or deletion of one or two based results in shifting of reading frame

Deletion of three bases

Protein CFTR (cystic fibrosis transmembrane) caused protein to not told properly and result in cystic fibrosis

Transposable elements

DNA sequences that move from one position to another in the genome


Transposons insert into genes and disrupt function

Chromosomal level insertion/ deletions

Duplication- region is present twice


Deletion- region is missing

Cri-du-chat syndrome

Deletion in chromosome


Effects one out of fifty thousand

Inversion

Normal order of block of genes is reversed


Two breaks in chromosome is flipped before breaks are repaired

Reciprocal translocation

Joins segments from different chromosomes


E.g. Chronic myelogenous leukemia results from part of chromosome 22 switching with small fragment from tip of chromosome 9

Lynch syndrome

One genes of mismatch repair is inactivated through mutations


More than 50% of people with Lynch syndrome develop colorectal cancer in their lifetime

BRCA1 BRCA2

Inherited


Increased probability of breast and ovarian cancer in women


Up to 50% of women with these gene mutations can develop breast and ovarian cancer in their lives


Products of BRCA genes involved in repair of DNA damaged by xray or UV Ray