Chp 2-4, 17 Test Flashcards

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1
Q

Types of bonds in water molecules (between H and O)

A

Polar covalent bonds between Hydrogen and oxygen molecules within the water molecule (the oxygen becomes negative and the hydrogen is positive)

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2
Q

Types of bonds in water molecules (between two water molecules)

A

Hydrogen bonds between the two water molecules (when a water molecule bonds to another water molecule through the hydrogen bonds is cohesion)

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3
Q

Ionic bond

A

the valence electrons are being transferred between a nonmetal and a metal (forms charges metal is positive and nonmetal is negative)

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4
Q

Covalent bond

A

the valence electrons are being shared between non metals to nonmetals
They are stronger than ionic bonds

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5
Q

Hydrogen bonds

A

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)

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6
Q

Van der Waals interaction bonds

A

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)

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7
Q

components of prokaryotic cells

A

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)

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8
Q

components of eukaryotic cells

A

Genetic material, plasma membrane, cytosol, ribosomes, linear DNA (located in the nucleus), membrane bound organelles (R?S ER, Golgi, etc), do not have plasmids

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9
Q

plasma membrane

A

regulates what enters and leaves the cell

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10
Q

nucleus

A

a vessel to hold the genetic material

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11
Q

nucleolus

A

produces/synthesizes ribosomes

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12
Q

rough endoplasmic reticulum

A

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

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13
Q

smooth endoplasmic reticulum

A

synthesizes/makes lipids, detoxifies drugs and proteins, metabolizes carbs, stores calcium ions (+2 charge)

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14
Q

lysosome

A

breaks down ingested substances and other cell macromolecules or damaged organelles to recycle them, has lysosomal/hydrolytic enzymes

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15
Q

golgi apparatus

A

sorts and packages materials into transport vesicles, modifies proteins, it can put carbohydrates and attach them to either proteins or lipids, synthesizes polysaccharides

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16
Q

peroxisomes

A

oxidated organelles, vessel that contains enzymes that transfer hydrogen to other molecules, makes hydrogen peroxide, breaks down hydrogen peroxide into water and oxygen gas

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17
Q

mitochondria

A

“powerhouse of the cell”, site of cellular respiration, makes ATP

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18
Q

chloroplast

A

process is photosynthesis to make sugar/glucose for the cell (glucose=the cells food)

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19
Q

cell wall

A

only in plant, fungi, and prokaryotes; to protect the cell, give the cell structure

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20
Q

ribosomes

A

protein synthesis

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21
Q

bonds found in carbohydrates

A

glycosidic linkage (formed by taking water out)

22
Q

bonds found in lipids

A

ester linkage (formed between the fatty acid chain and the OH group)

23
Q

bonds found in proteins

A

peptide bonds

24
Q

bonds found in nucleic acids

A

phosphodiester(form between the sugar and the phosphate groups on the backbone)

25
Q

when is a covalent bond likely to form

A

When valence electrons are shared (NM-NM)

26
Q

structure of an amino acid

A

Needs a central carbon, amino group, carboxyl, a hydrogen, an “R” group

27
Q

what determines amino acid chemical properties

A

The chemical properties are determined by its “R” group and what amino acid it is

28
Q

structure of a protein

A

CHON(S), always see an amine group (NH2)on one end and a carboxyl group (COOH) on the other end

29
Q

structure of a carbohydrate

A

CH2O, a lot of the time it is a ring structures

30
Q

structure of a lipid

A

CH2Oa few, fatty acid chain

31
Q

structure of a steriod

A

four fused ring structures

32
Q

structure of nucleic acid

A

CHONP, alternating phosphate group sugar and some sort of base

33
Q

structural isomers

A

if it is a structural formula it can have two different structures but the same formula, difference in covalent arrangement of the atoms

34
Q

geometric isomers

A

this forms when there are double bonded carbons, the orientation of the groups in relation to the double carbons can change

35
Q

enantiomers isomers

A

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)

36
Q

condensation reaction

A

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)

37
Q

hydrolysis reaction

A

breaks down polymers from large polymers to small monomers by adding H2O (happens in digestive system)

38
Q

pH concentration (in terms of H concentration, acid side, base side)

A

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

39
Q

what general classes of organisms are eukaryotes

A

plants, animals, protozoa/protists, fungi

40
Q

what general classes of organisms are prokaryotes

A

bacteria (EX: E coli, Salmanella, Staph aureus)

41
Q

what structures are part of the endomembrane system

A

(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)

42
Q

difference between a saturated fat (in terms of element make-up, bonds, found in plants or animals, solid or liquid at room temp)

A

maximum number of hydrogens are bonded to carbons on the chain, solid at room temperature, animal fats

43
Q

difference between a unsaturated fat (in terms of element make-up, bonds, found in plants or animals, solid or liquid at room temp)

A

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

44
Q

virus lytic cycle

A

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.

45
Q

virus lysogenic cycle

A

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)

46
Q

components of a virus

A

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

47
Q

what RNA viruses need to reproduce inside of a host cell

A

Need RNA (genetic material) and needs the enzyme reverse transcriptase

48
Q

function of reverse transcriptase

A

Programs host cell to convert viral RNA into DNA that can then be used as the code for protein synthesis

49
Q

4 steps in protein folding to make it functional (in terms of the types of bonds and what happens to the bonds)

A

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

50
Q

what is denaturation and what types of conditions cause it and how

A

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)