BIO test 1: Macromolecules and parts of the cell

carbon backbone, functional groups

what do all macromolecules have in common?

monomers

small, individual, similar subunits

• building blocks of macromolecules

polymer

chains of covalently linked monomers

polymerization

the process of monomers coming together to form polymers

Condensation/dehydration reaction

monomer in, water out

• add covalent bond

decreases, increases

when condensation reactions occur, entropy ___, and when hydrolysis occurs, entropy ____

hydolysis

water in, monomer out

• braks covalent bond

monosaccharides

monomers for carbohydrates

• simple sugars

i

isomers

molecules with the same chemical formula but different chemical structures

aldehyde group and oxygen

what causes a carbon ring to form?

alpha carbon

carbon one that has this configuration

beta carbon

carbon one that has this configuration

glucose

one main example of monosaccharides

polysaccharide

thousands of monosaccharide molecules attached to each other by covalent bond

glycosidic bond

what type of bond forms between monosaccharides?

lipids

largely nonpolar and hydrophobic

• composed primarily of C and H

• not technically a polymer

• chemically diverse

fats

triglycerides, lipids composed of fatty acids connected to a glycerol molecule

steroids

composed of many carbon atoms bonded to form rings

phospholipid

glycerol backbone, 2 fatty acid chains, and a phosphate containing head group

glycerol

3 carbon molecule with 3 hydroxyl groups

fatty acid

long unbranched chains of carbon and end with a carboxyl functional group

flexible

one quality of saturated fatty acids is that they are ____ and carbond atoms can rotate around the single bonds

3 fatty acids, glycerol

triacylglycerol is made of

energy storage

triglycerides are mainly for ____

ester bonds

bonds that form during condensation reactions for lipids

high

high carbon content, nonpolar bonds, has ____ chemical energy

saturated fat

• lots of hydrogen atoms

• straight and packed tightly

• high melting temp

• solid at room temp

unsaturated fat

• double nonds

• kinked

• not packed tightly

• low melting point

• liquid at room temp

hydrogenated oils

double bonds broken and hydrogen atoms added to give a certain structure

• more solid at room temp

amphipathic molecules

contain hydrophilic and hydrophobic regions

spontaneously, arrange

amphipathic molecules ___ arrange themselves in a way that ___ interactions with water to the hydrophilic part of the molecule

amino acids

monomers, subunits of proteins

central carbon, carboxyl group, amino group, hydrogen, variable group

what are amino acids made of?

alpha carbon

what is the name of the carbon in amino acids?

20

how many types of amino acids are there?

R group

determines the identity of each amino acid and its chemical properites when it is part at a larger protein

amino group, NH3+

when amino acids ionize, what becomes a base?

carboxyl group, COO-

when an amino acid ionizes, what becomes an acid ?

stay in solution and affect chemical reactivity

what does ionization of the amino group do?

hydrophilic

when amino acids have electrically charged or polar side chains they are ____

Determining amino acid properties

1. R-group negative charge? if yes=acidic

2. R-group positive charge? if yes=basic

3. R-group uncharged with oxygen atom? if yes=polar

4. r-group uncharged with no oxygen? if yes=nonpolar

peptide bond

the kind of bond is formed between amino acids in polypeptides

• covalent bond

amino and carboxyl

between what two groups does a condensation reaction occur in amino acids?

residue

individual amino acid

polypeptide

chain of amino acids

• more than 20 AA

side chains

what part of polypeptides interact with water and each other?

directionality

monomers attached in the same orientation form their end terminus to their C terminus

amino terminus

free amino group at one end when linked to form polypeptides

oligoprotein

a few amino acids linked together

• fewer than 20 AA

protein

any chain of AA residues

• refer to the complete, functional form of the polypeptide

primary protein structure

the unique sequence of amino acids in the polypeptide, form the N-terminal to the C-terminal end

• single change in AA impact the way a protein behaves

• R-groups affect chemical reactivity and solubility of protein

• common to all proteins

secondary protein structure

created by interactions (hydrogen bond) between Carboxyl=Oxygen and Amino group-H functional groups of different residues

• a-helix

• B-sheet (pleated)

Tertiary Protein Structure

due to the interactions that involve atoms on the side chain of amino acids

• hydrogen bonds btwn R and carboxyl

• hydrophobic interactions: NP substance to aggregate

• disulfide bond

• ionic bond

disulfide bond

between cysteine residue and side chain

quarternary structure

two or more polypeptides assemble to form a larger protein molecule

folding

what is crucial to a protein’s function?

chaperones

specialized proteins that help other proteins fold correctly

Ex: heat shock proteins help refold proteins denatured by high temps

prion

infectious disease causing agents that were once normal proteins that were induced into incorrect folding

• can cause a chain reaction

selective permeability

lipid bilayers have ___

higher; lower

lipid bilayer with short and unsaturated hydrocarbon tails have ___ permeability and fluidity, while one iwth long and saturated hydrocarbon tails have ___

lipoproteins

spherical structures made of phospholipids

extracellular fluid

keep stuff you don’t need outc

cytoplasm

keeps the stuff you need in

fluid mosaic model

the cell membrane is fluid and flexible with lateral movement of lipids or proteins and diverse arrangement

lipid composition , temperature

membrane fluidity depends on ____

transmembrane proteins

span the entire bilayer

integral proteins

embedded in bilayer

• can be hydrophobic and hydrophilic

peripheral membrane proteins

associated with one face

anchored membrane protein

covalently bonded to lipids that are inserted intot he membrane

glycoprotiens

carbohydrate attached to the outer surface of proteins

glycolipids

carbohydrates are attached tot he outer surface of lipids

recognition sites

interact with external environment

detergents

amphipathic, water soluble molecules that can form micelles

• hydrophobic tails of _____ molecules interact with hydrophobic portions of transmembrane proteins to allow isolation

surface carbohydrates

• thought of as a molecular signature

• allow cells to be identifiable based on their surface features

cell structure

• plasma membrane

• proteins perform most cell functions

• carbohydrates provide energy and support

• contain genetic material

• cytoplasm and ribosomes

prokaryotic cells

• don’t have membrane bound organelles

• no nucleus

• unicellular: bacteria and archaea

• small

• DNA in nucleoid

• may have plasmids

• cell wall

plasmids

contain genes but are physically independent of the main chromosome

• help adapt to unusual circumstances

flagella

swimming

fimbriae

attachment to other cells or surfaces

eukaryotes

• eukarya—4 kingdoms

• multicellular and unicellular

• contain organelles

• has a nucleus

organelles

specialized internal compartments defined by membranes

compartmentalization

division of labor efficiency and regulation

domain eukarya

• protists

• fungi

• plants

• animals

endomembrane system functions

1. carry and direct newly synthesized proteins

2. make necessary modifications to the proteins as they are moved

nucleoulus

• where RNA is manufactured

• Ribosomal subunits are also assembled here

Nuclear envelope

double membrane (inner and outer) and has nuclear pores

smooth ER

site of lipid production, detoxification

rough er

associated with ribosomes that are synthesizing proteins

• studded with ribosomes

endoplasmic reticulum

• wraps around the nucleus

  • smooth and rough

ribosomes

macromolecular machines that manufacture proteins

• composed of protiens and RNA

• for eukaryotes it is scattered in cytosol and is associated with ER

• not considered an organelle or part of the endomembrane system

golgi apparatus

stacks of flat membrane bound sacs (cisternae)

• modify proteins, lipids

• cis face to trans face

• receives from ER

• directs proteins and lipids to other organelles

• uses glycosylation

glycosylation

attachement of small carbohydrates

• glycolipids and glyoproteins

lysosome

recycling center of the cell

• part of endomembrane system

• enzymes break down biomoleules that are damaged, defective, or no longer needed

• perform hydrolysis

• integral membbrane proteins pump protons into here

mitochondrion

• two membranes

• supplies energy in the form of ATP

• has its own DNA

chloroplast

• 2 membranes

• converst sunlight into chemical energy with photosynthesis

• contains copies of its own chromosome

mitochondria, chloroplast

which two organelles are believed to be once free living bacteria and have their own dna

vacuoles

very large, found in pants, fungi and some other eukaryotes where lysosomes are not present

• storage depots

peroxisomes

contain enzyme that catalyze oxiddation reactions important for cellular function

nucleus

• largest organelle

• surrounded by nuclear envelope with pores

• DNA and helps with transcription and assembles ribosomes