Campbell Biology: Ch 2-5 test 1 Flashcards


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Campbell Biology
Chapters 2-5
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1

What makes each element unique and different from other elements

Unique number of protons

2

What is the significance of atomic number

atomic mass?

Atomic number tells us the amount of protons in an atom

atomic mass tells us how many neutrons by subtracting the amount of protons

electrons can be found in the electron cloud. 1-2 On periodic table: electrons. 13-18 find by subtracting 10

3

What are isotopes

Variants of a particular element

different # of neutrons same # of protons

4

Atoms octet

If there are a certain number of electrons in an electron cloud you can either add or give away electrons to complete a perfect octet through sharing of electrons between elements

5

What are the max number of bonds specific elements can make?

Single H-H. Double bond= 2 pairs of electrons

double O= O. Triple bond= 3 pairs of electrons

triple N=_N

6

Define electro negativity

Level of charge given from one atom to attract another. Book Def: the attraction of a particular atom for the electrons of a covalent bond

7

How can electronegativity effect covalently bonded molecules

It takes partially greater charges from either positive and negatively bonded atoms and while shared equally, electrons will stay closer to the more electronegative charge

8

What happens if the electronegativity is equal

There is a standoff of tug of war and a non polar covalent bid is formed

9

What is the difference between ionic and covalent bonds?

Ionic bonds= electrons are not shared equally

covalent bonds= electrons are shared equally

10
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Because it will gain one electron

11

Structure of water - hydrogen bond, polar covalent bond, explain in detail partial negative charge of water molecule and why it occurs in terms of electronegativity and electrons

Positive H in one H2O molecule attracts to negative O in another. Polar covalent bond = partially negative/positive binding in a covalent bond and the electrons stay closer to the more electronegative side

12

Importance of hydrogen bonding to the properties of water

Hydrogen bonds form the basic structure of water for other bondings such as polar covalent to occur

13

Why do carbon atoms form diverse molecules

Carbon has 4 valence electrons do it can share electrons with other diverse molecules

14

Hydrophobic molecules and how they interact with water

Hydrophobic doesn’t dissolve in water. It is no polar and does not have an attraction to water

15

Interpret a PH scale

1-6 Acid 7 neutral 8-14 basic

16

The importance of buffers in biological systems, how do they balance PH?

They maintain a relative constant PH when either acids or bases are added to them

17

The role of dehydration reaction in organic compounds and hydrolysis in digestion of organic compounds

Dehydratiom reaction: assembles polymers releasing H2O

Hydrolysis: breaks down polymers consuming H2O

18

The four macromolecules and bonds that are formed durning the dehydration reaction

Carbohydrates: glycoscidic linkage

Lipid: ester linkage

nucleic acid: phosphodiester linkage

protein: peptide bond

19

Classify monosaccharides, disaccharides, and polysaccharides

Monosaccharid: monomer of carbohydrate ex: lactose glucose

Disaccharide: two monosaccharides ex: sucrose

polysaccharid: polymers ex: plants -store glucose as starch, animals -glycogen, cell structure in plants -cellulose

20

The difference between starch and cellulose and how it impacts digestion

Starch: stores energy in plants. Plants and animals can digest

cellulose: structural component in plants. CANNOT be digested by animals on account of beta glucose linkage

21

What’s the difference between saturated and unsaturated fats

Unsaturated: liquid, at least on double bond

saturated: solidify, contains more hydrogen,only single bonds, contributes to atherosclerosis (heart disease)

22

What is the first structural level of protein? How can it change the activity of the protein

Primary: A mess up will ruin all other structures. It dictates secondary and tertiary structure. Linear chain of amino acids

23

Second structural level of protein

Secondary: hydrogen bonds between an amino group of one peptide bond and the carbonyl group of another peptide bond

24

Third structural level of proteins

Tertiary: interaction between r groups. Disulfide bridge, ionic bond, hydrogen bond between at least one r group

25

Fourth structural level of proteins

Quaternary: two or more polypeptide chains into one large protein

26

What makes each amino group different from one another?

Each has a different R group

27

Name the bonds that are formed in primary and secondary structures of proteins

Primary: peptide

secondary: hydrogen

28

Identify the peptide bond if given a polypeptide:

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Carbon with a double bond to an oxygen single bonded to carbon attached to Nitrogen

29

What maintains structure of a protein

Hydrogen bonds

30

What is chaperonin

They help fold proteins within cells in the last structural level of proteins

31

Base pairing rules of DNA

A=T

C=G

32

Steroid structure

4 carbonn fused rings

33
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34

Hydrocarbons are not soluble in water because

The C—H bond is nonpolar

35

What molecul a form a triacylglycerol/fat know and recognize the structure

G

l. Fatty acid 1

y

c

e. Fatty acid 2

r

o

L. Fatty acid 3

36

Bond between nucleotide to make nuclei acids - reaction forms it, type of bond

Phosphodiester covalent bond to form backbone from 5’ carbon and 3’ carbon

37

Recognize the the four biologically important organic compounds

Carbon

Hydrogen

Oxygen

Nitrogen

38

How do proteins reach their final shape

They go through all four phases and complete by using chaperonins