Biology Exam 1

Biology 101 with Thoma at University of Wisconsin - Madison

About this deck

By: Meryl Sell
Textbook:

Biology with MasteringBiology? (8th Edition)
Created: 2011-02-16
Size: 107 flashcards
Views: 145

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What is life?

ORRRGEE

Order, Regulation, Reproduction, Response to Environment, Growth and development, Evolutionary adaptation, Energy processing

Levels of biological organization

atom, molecule, organelle, cell, tissue, organ, organ system, organism, population, community, ecosystem, biosphere

Classification of organisms. Chart of classification.

Kingdoms: Protista, Animalia, Fungi, Plantae

Eukaryotic Prokaryotic

Domians: Eukaryea Bacteria Archaea

Cytochrome C

Found in all aerobic organisms.

Crucial for making ATP

Natural Selection

Weak organisms die, strong ones live on so the population evolves.

Covalent bond

A bond where atoms share a pair of electrons

Electronegativity trends and symbol

Increasing from lower left of the periodic table to upper right

S- is more electronegative, electron is closer to this molecule

S+ is less electronegative

Polar covalent bond

When the two electrons in a bond are shared unequally because of electronegativity. Look at each atom in a molecule and where it is on the periodic table and relate their electronegativities to all of them.

H bond

Hydrogen bond, when molecules are attracted to each other because of electronegativity and form mini bonds. The bonds form between hydrogen and either Oxygen, Nitrogen, or Sulfur, and only when Oxygen, Nitrogen, or Sulfur are electronegative (S-).

Property of "organic"

contains carbon

Organic macromolecules

Carbohydrates, proteins, lipids, nucleic acids

Structure of a macromolecule

HO - R - R - R - R - H

How are macromolecules built?

Dehydration synthesis.

HO - R - H + HO - R - H ---> HO - R - R - H + H2O

Caused by enzyme polymerase.

What are polymer's made of and what types of polymers are there?

Monomers.

Dimer = 2 monomers

How are macromolecules broken down?

Hydration synthesis and enzymes.

HO - R - R - H + H2O -----> HO - R - H + HO - R - H

Carbohydrate features

carbon hexagon with one oxygen in place of a carbon

H and OH connected to every carbon except one

Monomer's connected with O

Carbohydrate monomer

Saccharide

Function of disaccharides, examples of disaccharides

Sucrose, lactose, maltose

Broken down by hydrolytic enzymes for quick energy

Examples and functions of carbohydrate polysaccharides

Starch - energy storage for plants

Glycogen - energy storage for animals in the liver

Cellulose (fiber) - structure for plant cells

Which carbohydrate polysaccharides can be broken down by hydrolytic enzymes?

starch and glycogen

Protein monomer

amino acid

Protein structure

Carbon in center:

Amino group on one side H N H

Carboxyl (acid) group on one side O C OH

H on one side

R on one side

How many different R groups and amino acids are there?

How can you tell if an amino acid is charged?

If there is a + or a - in the R group

How can you tell if an amino acid is hydrophilic?

If the molecule is charged

If the molecule has a polar covalent bond OH SH NH (H2O soluble)

How can you tell if an amino acid is hydrophobic?

Does not have a polar covalent bond of OH SH NH

What are the bonds between amino acids, and what are many amino acids called?

Peptide bonds

Dipeptide

Polypeptide

What is a functional protein?

A folded up polypeptide

What are the four levels of protein structure?

Primary structure

Secondary structure

Tertiary Structure

Quaternary Structure

What is a protein primary structure?

The linear sequence of amino acids

What is a protein secondary structure and what are the types?

Local folding of the linear sequence of amino acids

Alpha helix bonding: swirly

Beta Pleated sheet: folding in half, zig zag

H bonding

What is a protein tertiary structure and how does it form?

Forms globs

Held together by hydrogen, ionic, and hydrophobic interactions

Hydrophilic amino acids in outside

Hydrophobic amino acids on inside

Lysozyme

Kills bacteria

Soluble protein with hydrophilic amino acids on outside

hydrophobic amino acids on inside

What is a protein quaternary structure, what are they composed of, and how are they held together?

When two polypeptides are combined

Composed of alpha and beta chains (secondary structure)

Iron hemes hold them together

Characteristics of enzymes and how they work

Enzymes speed of rates of reactions

Reusable

1. Attach to substrate

2. Break the bond of the substrate

3. Detach from the substrate

4. Repeat

When do enzymes not work?

When denaturation happens

Temperature and pH are off

pH scale in brief

0 acidic high in H+ concentration

14 basic high in OH- concentration

Lipid functions

GUMIER

Growth, Uses vitamins, cell Membranes, Insulation, Energy soruce, Regulatory function

What are the 3 types of lipids?

Sterols (steroids), Fats and oils, Phospholipids

Lipid sterol structure and function

Four rings attached side to side

Hormone - estrogen, testosterone, cortisol

Membrane structure - cholesterol

What is an apolipoprotein and what is its function?

Cholesterol is hydrophobic

A ring of phospholipids

Triglycerides in the middle

Cholesterol in between the phospholipids

Moves cholesterol throughout the blood stream

What are the two types of lipoproteins and how do they differ?

Low density lipoprotein (LDL) - lazy=bad, bad cholesterol, makes plaque in arteries

High density lipoprotein (HDL) - happy=good, good cholesterol, can offset LDL

Fats and Oils: Triglyceride (fat) structure

Glycerol + 3 fatty acid hydrocarbon tails, all hydrophobic

H O HHHHHHHHH

HCOC CCCCCCCCCCCH

HHHHHHHHH

O HHHHHHHHH

HCOC CCCCCCCCCCCH

HHHHHHHHH

O HHHHHHHHH

HCOC CCCCCCCCCCCH

H HHHHHHHHH

Fatty acid chains are connected to glycerol by dehydration synthesis

Saturated and Unsaturated fats

Saturated - no double bond, packed tightly, solid, increase HDL and LDL

Unsaturated - one double bond, not tight, liquid, better for you

Polyunsaturated - more than one double bond, even better for you

Trans and cis fats, hydrogenation, partial hydrogenation

To get trans: add hydrogen to vegetable oil through hydrogenation

Adding hydrogen eliminated double bonds making the molecule more dense and solid

Partial hydrogenation changes some cis to trans

Trans: hydrogen on opposite sides

Cis: hydrogen on same side

Phospholipid facts

component of cell membranes

hydrophilic phosphate head

hydrophobic 2 fatty acid tail

glycerol in middle

amphipathic - both hydrophilic and hydrophobic

Types of phospholipid forms

Micelle - A ball of phospholipid that occurs in water

Lipoprotein complex - Carries around cholesterol

Phospholipid bilayer (liposome) - plasma membrane

Functions of the plasma membrane

regulates what enters and leaves the cell, selectively permeable

maintains shape of cell

controls interactions between cells

Characteristic of plasma membrane

Phosphate and some proteins move fluidly

More fluid = more permeable

Effects on temperature, saturation of hydrocarbon tails, length of hydrocarbon tails, and cholesterol on permeability

Temperature: Temp goes up, fluidity/permeability goes up

Saturation of hydrocarbon tails: more saturated, less fluid/permeable, more unsaturated, more fluid/permeable

Length of hydrocarbon tails: longer tail --> stronger hydrophobic interactions, less fluid/permeable

Cholesterol: no cholesterol, most fluid/permeable

50% cholesterol, less fluid/permeable

at low temperatures it's opposite

Membrane protein structure

TRACES

Transport, cell-cell Recognition, Attachment, Cell joining, Enzymes, Signaling

Types of passive transport

Simple diffusion, facilitated diffusion, osmosis

Types of membrane transport

passive transport, active transport, vesicular (bulk) transport

Simple diffusion

movement down the concentration gradient

hydrophobic

uncharged

steroids

O2 CO2 NO2 (H2O)

NOT large

NOT polar

NOT ions

Facilitated Diffusion

movement down the concentration gradient

movement aided by proteins

channel protein: a channel for substances to go through

carrier protein: open to take substance in, opens in other direction to move substance to inside of cell

Osmosis

passive transport of water, water moves down its concentration gradient

combination of simple diffusion and facilitated diffusion

Hypotonic, hypertonic, isotonic

hypotonic: lower concentration of SOLUTE

hypertonic: higher concentration of SOLUTE

isotonic: same concentration of solute in water

aquaporins

water channels in the plasma membrane to move water in an out of the cell, used in osmosis sometimes

Active transport

movement against the concentration gradient

energy is used ATP

sodium/potassium pump

ATP structure and ADP

Three phosphate groups containing O and P

1 Ribose containing a pentagon, H O and 1 C

1 adenine containing a pentagon and hexagon, H C N

ADP=ATP+P

same as ATP except two phosphate groups

Sodium/potassium pump

Na+ from inside cell put in transport protein

ATP makes P+ADP, & P is added to protein

P moves protein,sodium is released outside

K+ from outside is put in protein

The P leaves the protein

protein moves to original position

K+ released to inside of cell

Cystic fibrosis and CFTR protein

CFTR is mutated and doesn't move Cl- or H2O so the mucus doesn't thin

Vesicular (Bulk) Transport

Movement of substances into and out of the cell by vesicles

Exocytosis and endocytosis

Vesicular (Bulk) Transport

exocytosis: substances released from cell

endocytosis: substances put in cell

Types of endocytosis

Phagocytosis, pinocytosis, receptor-mediated endocytosis

breaks off into vesicle

lysosome attaches to vesicle and destroys any bad things

Phagocytosis

Eating something big

non-selective

big molecules, cells

Pseudopodium is formed around big object

Pinocytosis

little things eaten

dissolved molecules

non-selective

Receptor-mediated endocytosis

membrane protein receptors grab certain substances

once the substances are grabbed its the same ad pinocytosis

on the other side of the membrane protein receptors are coat proteins

uptakes LDL cholesterol into cells

karyo, Eu, Pro

karyo - nucleus

eu - true

pro - before

flagella

power, movement

ribosomes

make proteins

cytoplasm

hypertonic to environment

chromosome

in nucleoid region, contains genes

plasmid

genes that help cells survive unusual situation (medication)

reasons why some bacteria/prokaryotes are good

mutualism, decomposition, competition with bad bacteria, helps development

archaea

extreme environments - extremophiles

Eukaryotic cells and diffusion

diffusion problem because they are so big

solution=compartmentalization, organelles

Nucleus parts

nuclear envelope: outside part of nucleus

nucleoplasm: the stuff inside the nucleus

chromatin: DNA + protein

nucleolus: dark middle part of nucleus

nuclear lamina: stringy things

ER: stuff around nucleus

nuclear pores: where stuff moves in and out

Nuclear lamina function and structure

function: shapes nucleus, organizes chromatin

structure: lamins - intermediate filaments

lamin - associated membrane proteins

lamin filament made of lamin dimers with lamin associated proteins in it

NLS

proteins destined to go to nucleus have nuclear localization signal

cytoskeleton

cell skeleton

Endoplasmic reticulum

biosynthetic factory

secreted proteins enter ER as they are veing synthsized by ribosome

protein exits ER in vesicle

protein synthesis

1. secreted proteins enter ER as they are being synthesized by ribosome

2. protein exits ER in vesicle

3. protein travels through the cisternae of the Golgi apparatus

4. protein enters a secretory vesicle that fuses with cell membrane

5. protein is secreted from cell

How does a protein know to go into the ER?

cellular zip code

What happens to the protein in the ER?

protein folding

glycosylation, addition of oligosaccharide --> glycoprotein

How do proteins get from ER to golgi?

transport vesicle

What happens inside the Golgi apparatus?

modifications of protein

sorting

shipping to outside of cell

Lysosomes

digestive compartments

digest materials in the cell or fuse with endocytic vesicles

Types of cytoskeleton

microfilament - twisted, microtubule - tube, intermediate filament - twisted tube

Motor proteins

carry the transport vesicle along the microtubule from the ER to the golgi cis face

Peroxisomes

oxidation

breakdown of molecules

macromolecule --> degrading enzyme --> breakdown products and H2O2 --> catalase --> H2O + O2

mitochondria

sites of cellular respiration

chloroplasts

sites of photosynthesis

extracellular matrix

outside the cell

animal cells

composed of glycoproteins

structural support

anchorage for cells

regulation of intracellular communication

cell wall

plant cells

structural support

protection

two types of nucleic acid

DNA

RNA

nucleic acid monomer

nucleotide

structure of nucleotide

phosphate group OOOOP

pentose sugar CCCCO

nitrogenous base N

DNA and RNA bases

DNA CG TA

RNA CG UA

DNA and RNA sugars

DNA deoxyribose

RNA ribose

DNA and RNA location

DNA nucleus

RNA nucleus and cytosol

null

DNA replication process

1. Parent molecule is double stranded, antiparallel

2. strands are separated and each strand is a template

3. Daughter molecules are made

Telomeres

do not contain genes

short stretches of bases repeated over and over

found in stem cells, embryonic cells

cells without telomerase will get shorter chromosomes with each division

limit of 40 cell divisions --> cell death

telomere replication

1. the end of a parent DNA remains unreplicated

2. telomerase binds to the unreplicated part

3. telomerase moves down dna strand and adds additional nucleotides

4. primase, DNA pol, ligase make it into two strands in the 3' direction

helicase

unwinds the DNA for replication

Lagging strand replication

1. RNA primase prepares strand in 5' direction

2. DNA polymerase III makes DNA in the 3' direction in between the RNA segments

3. DNA polymerase I replaces III and makes the RNA segments into DNA

About this deck

By: Meryl Sell
Textbook:

Biology with MasteringBiology? (8th Edition)
Created: 2011-02-16
Size: 107 flashcards
Views: 145

About StudyBlue

“Simply amazing. The flash cards are smooth, there are many different types of studying tools, and there is a great search engine. I praise you on the awesomeness.”
Dennis