Chp 2-4, 17 Test Flashcards
Types of bonds in water molecules (between H and O)
Polar covalent bonds between Hydrogen and oxygen molecules within the water molecule (the oxygen becomes negative and the hydrogen is positive)
Types of bonds in water molecules (between two water molecules)
Hydrogen bonds between the two water molecules (when a water molecule bonds to another water molecule through the hydrogen bonds is cohesion)
Ionic bond
the valence electrons are being transferred between a nonmetal and a metal (forms charges metal is positive and nonmetal is negative)
Covalent bond
the valence electrons are being shared between non metals to nonmetals
They are stronger than ionic bonds
Hydrogen bonds
a bond between the hydrogen attraction (hydrogen will have a slight positive) between an electronegative atom/side of the molecule (normally an electronegative atom such as Oxygen and Nitrogen)
Van der Waals interaction bonds
regions of positive and negative charges that stick molecules together, very weak, regions do not necessarily stay in their place at all times (more of an intermolecular force)
components of prokaryotic cells
Genetic material, plasma membrane, cytosol, ribosomes, circular DNA (located in the nucleoid region), does not have any membrane bound organelles, they can have plasmids (little circular pieces of DNA that hold a few genes)
components of eukaryotic cells
Genetic material, plasma membrane, cytosol, ribosomes, linear DNA (located in the nucleus), membrane bound organelles (R?S ER, Golgi, etc), do not have plasmids
plasma membrane
regulates what enters and leaves the cell
nucleus
a vessel to hold the genetic material
nucleolus
produces/synthesizes ribosomes
rough endoplasmic reticulum
helps in the folding process of the proteins that eventually go to the outside of the cell, helps make membranes (membrane synthesis), aids in the synthesis of secretory proteins, also adds carbs to proteins to make glycoproteins
smooth endoplasmic reticulum
synthesizes/makes lipids, detoxifies drugs and proteins, metabolizes carbs, stores calcium ions (+2 charge)
lysosome
breaks down ingested substances and other cell macromolecules or damaged organelles to recycle them, has lysosomal/hydrolytic enzymes
golgi apparatus
sorts and packages materials into transport vesicles, modifies proteins, it can put carbohydrates and attach them to either proteins or lipids, synthesizes polysaccharides
peroxisomes
oxidated organelles, vessel that contains enzymes that transfer hydrogen to other molecules, makes hydrogen peroxide, breaks down hydrogen peroxide into water and oxygen gas
mitochondria
“powerhouse of the cell”, site of cellular respiration, makes ATP
chloroplast
process is photosynthesis to make sugar/glucose for the cell (glucose=the cells food)
cell wall
only in plant, fungi, and prokaryotes; to protect the cell, give the cell structure
ribosomes
protein synthesis
bonds found in carbohydrates
glycosidic linkage (formed by taking water out)
bonds found in lipids
ester linkage (formed between the fatty acid chain and the OH group)
bonds found in proteins
peptide bonds
bonds found in nucleic acids
phosphodiester(form between the sugar and the phosphate groups on the backbone)
when is a covalent bond likely to form
When valence electrons are shared (NM-NM)
structure of an amino acid
Needs a central carbon, amino group, carboxyl, a hydrogen, an “R” group
what determines amino acid chemical properties
The chemical properties are determined by its “R” group and what amino acid it is
structure of a protein
CHON(S), always see an amine group (NH2)on one end and a carboxyl group (COOH) on the other end
structure of a carbohydrate
CH2O, a lot of the time it is a ring structures
structure of a lipid
CH2Oa few, fatty acid chain
structure of a steriod
four fused ring structures
structure of nucleic acid
CHONP, alternating phosphate group sugar and some sort of base
structural isomers
if it is a structural formula it can have two different structures but the same formula, difference in covalent arrangement of the atoms
geometric isomers
this forms when there are double bonded carbons, the orientation of the groups in relation to the double carbons can change
enantiomers isomers
mirror images of each other, two forms are L form or D form (basically left and right form), can make a huge difference (EX: thalidomide: given for pregnant women for morning sickness and the mirror images cause birth defects)
condensation reaction
builds polymers by taking a H group from one and an OH group from another and creating water and the bond (happens in digestive system)
hydrolysis reaction
breaks down polymers from large polymers to small monomers by adding H2O (happens in digestive system)
pH concentration (in terms of H concentration, acid side, base side)
0-14, each number represents the logarithmic hydrogen ions/hydroxide, acids=<7, bases=>7, 7=neutral, an acid has higher hydrogen ions than hydroxide ions, neutral hydrogen and hydroxide ions are equal, bases hydroxide ions are greater than the hydrogen ions
what general classes of organisms are eukaryotes
plants, animals, protozoa/protists, fungi
what general classes of organisms are prokaryotes
bacteria (EX: E coli, Salmanella, Staph aureus)
what structures are part of the endomembrane system
(Inside-Out)
Nucleur envelope
Endoplasmic Reticulum
Golgi Apparatus (not directly attached to ER, a vesicles connects them)
Lysosome/Peroxisomes (vesicles created by GA)
Plasma membrane (vesicles will become part of the membrane or fuse and dump contents out of the cell)
difference between a saturated fat (in terms of element make-up, bonds, found in plants or animals, solid or liquid at room temp)
maximum number of hydrogens are bonded to carbons on the chain, solid at room temperature, animal fats
difference between a unsaturated fat (in terms of element make-up, bonds, found in plants or animals, solid or liquid at room temp)
double bonds between carbons; therefore, there are not the maximum number of hydrogens bonded to carbons on the chain, liquid at room temperature, general found in plants or fish, generally oils, double bond causes bend
virus lytic cycle
the virus injects into host cell/fuses with the membrane, the genetic material programs the host cell to make virus parts, the host cell assembles those virus parts and when they are fully assembled it breaks open (lyses) the cell and releases them, resulting in the killing of the cell.
virus lysogenic cycle
the injected DNA gets incorporated into the host genome and stays there as a prophage until conditions inside the cell are right for the virus to then enter the lytic cycle
(when/if conditions aren’t good, conditions stay dormant and does not harm or do anything to the cell)
components of a virus
Two: capsids (made out of proteins called capsomeres) and genetic material in the form of single or double stranded DNA or single stranded or double stranded RNA
what RNA viruses need to reproduce inside of a host cell
Need RNA (genetic material) and needs the enzyme reverse transcriptase
function of reverse transcriptase
Programs host cell to convert viral RNA into DNA that can then be used as the code for protein synthesis
4 steps in protein folding to make it functional (in terms of the types of bonds and what happens to the bonds)
Primary Structure:
Along change of amino acids that are formed at the ribosomes and are linking/bonding together by a condensation/dehydration reaction (releases water)
Secondary Structure:
The alpha helix (curly Q) and the beta pleated sheets (fan folding) that are caused by hydrogen bonds between amino acids
Tertiary Structure:
Much more folded due to R group interactions: disulfide bridges form between amino acids called cysteine (one cysteine will find another cysteine and create the bridge), ionic bonds (between positive and negative charged R group), hydrophobic and hydrophilic reactions of the R groups (hydrophilic goes to outside)
Quaternary Structures:
Two or more polypeptides in the tertiary structures are bonded together
what is denaturation and what types of conditions cause it and how
Denaturation is the unravelling/unfolding of the protein.
Temperature (causes movement) helps to break the bonds, pH (because it is a concentration of hydrogen ions and positively charged), salt (the ions will mess with the bonding, the negative will get pulled to the positive and cause the unraveling)
