bio 211 - exam 1

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Last updated 6:09 AM on 4/24/26
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64 Terms

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atomic structure and bonding

nucleus with protons (positive) and neutrons (neutral)

  • - surrounding orbitals contain negative electrons

  • - number of bonds an atom can form is based on the number of spaces in its valence shell

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covalent bonds

sharing electrons between atoms

nonpolar: electrons shared equally

polar: electrons are unequally shared because one atom attracts electrons stronger than the others

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electronegativity

the strength an atom pulls electrons with

  • if two atoms have similar electronegativity, they form nonpolar bonds, otherwise, polar bonds are formed

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ionic bonds

electrons are transferred from one atom to another

  • typically found between metals and nonmetals

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hydrogen bonds

from between and H atom (with a slightly positive charge) and an atom with a partial negative charge

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van der Wall interactions

form between hydrophobic molecules when they create opposing charges in each other, causing attraction

  • - occurs when nonpolar molecules are in close proximity to each other

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isomer

compounds with the same molecular formula but different arrangements of atoms

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hydroxyl group

-OH

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ketone group

carbonyl in the middle of a carbon chain

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aldehyde group

carbonyl at the end of a carbon chain

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amine group

NH2

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carboxy group

COOH

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macromolecule

large organic (contain carbon) molecules that carry out specific functions

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what are the four classes of macromolecules?

carbohydrates, nucleic acids, proteins, lipids

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monomer

building blocks that make up molecules

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polymer

long molecules made up of repeating monomers

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dehydration synthesis/condensation reactions

connects two monomers, water molecule is formed (OH from one monomer, H from the other)

  • - endothermic reaction because energy is stored in the bond formed

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hydrolysis reaction

polymer breaks up into two monomers using a water molecule

  • -exothermic reaction (energy from bond is released)

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what is the carbohydrate monomer and bond that connects them?

monosaccharides, connected by glycosidic bonds

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what is the nucleic acid monomer and bond that connects them?

nucleotides, which are connected by phosphodiester bonds

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what is the protein monomer and bond that connects them?

amino acids, which are connected by peptide bonds

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what is the protein monomer and bond that connects them?

no monomer, various single and double bonds connection portions (ester linkages connect triglycerides)

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amino acid structure

  • alpha carbon in the center

  • amine group to the left

  • R group below the alpha carbon

  • carboxy group to the left

end amine group is the N-terminus, C terminus is the carbon end

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what are the three main chemical properties of r groups?

electrically charged, polar, or nonpolar

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Electrically charged r groups

can be acidic or basic

  • - acidic groups will have a COOH bonded to some CH..

  • - basic groups will have CH bonded to one or more NH

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polar r groups

allow r groups to form hydrogen bonds with water

  • - have CH or OH, or CH-C-O-NH2

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nonpolar r groups

don’t interact with water

  • - have H, CH, S, NH, can be long or short

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peptide bond formation

oxygen form carboxyl group combines with two hydrogens from an amine group, forming water and a —

  • - lone pairs on N give this bond the characteristics of a double bond and make it more stable

  • - R groups face away from the backbone

  • - single bonds make backbone flexible for folding

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levels of protein structure

primary, secondary, tertiary, quaternary

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primary protein structure

refers to the polypeptide chain, which is held together by peptide bonds

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secondary protein structure

formed by hydrogen bonding between portions of the polypeptide chain (no R groups involved)

  • - forms alpha helices and beta pleated sheets

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tertiary protein structure

formed by interactions between R groups, including ionic, hydrogen, disulfide, hydrophobic, and van der Waal bonds/forces

  • - occurs over long ranges to form intricate structures

  • occurs between beta sheets, alpha helices, and disulfide bonds

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quaternary protein structure

occurs when multiple polypeptide subunits interact, forming, dimers, trimers, etc.

  • - can be between the same or different subunits

  • - same bond types as tertiary structure

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factors affecting protein folding

  • - can be denatured by acids, bases, heat, salt, reducing agents

  • - may undergo confirmational changes in response to environmental conditions or to interact with other proteins

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nucleotide structure

made up of:

  • one phosphate group that gives it a negative charge

  • one five carbon sugar (ribose or deoxyribose)

  • a nitrogenous base (A, T, G, C, or U)

aka NTP (— triphosphate monomers)

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nucleotide base pairing

a forms double bonds with t

g forms triple bonds with c

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purines

have a two ring structure

  • guanine and adenine

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pyrimidines

have a one ring structure

  • cytosine, thymine, and uracil

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how are phosphodiester linkages formed

the hydrogen atom of a hydroxyl group on 3’ carbon combines with hydroxyl from phosphate group to form a water molecule

  • linkage forms from 3’ carbon to a phosphate and a phosphate to a 5’ C of the next sugar

  • - the 5’ end has a terminal phosphate, whereas the 3’ end has a terminal hydroxyl group

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features of DNA

  • exhibits antiparallel orientation (one strand runs from 3’ to 5’, the other from 5’ to 3’)

  • one helical turn is about 10 base pairs long

  • helix is 2nm wide, with .34 nm between base pairs

  • helix has alternating major and minor grooves (proteins use H bond donors and acceptors to find binding site on major groove

  • g forms triple bonds with c and a forms double bonds with t

  • h bonds and van der Waal forces help to strengthen attraction between bases

  • is right handed

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What are the differences between RNA and DNA

— uses a, g, c, t whereas — uses a, c, g, u

— uses deoxyribose, which doesn’t have a hydroxy group on the second carbon, whereas — uses ribose

— is double stranded, whereas — is single stranded but can fold to become double/triple stranded

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why is RNA unstable

it can undergo self-hydrolysis of its sugar backbone

  • the 2’ OH attacks phosphate, breaking the bond between the phosphate and the other sugar its bonded to, breaking the chain

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evidence for an RNA world

riboenzymes are — molecules that can catalyze reactions requiring enzymes, meaning there could be a world where — was self sufficient (genetic material and could catalyze reactions, forming life)

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monosaccharide structure and numbering

made up of carbonyl and OH groups

  • if the carbonyl is at the end of the C chain, its an aldose

  • if the carbonyl is in the middle of the C chain, its a ketose

  • C’s are numbered starting with the one closest to the carbonyl group

  • 3 C = triose, 5 = pentose, 6 = hexose

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how do sugars go from linear to ring structure

carbonyl group on one carbon reacts with a hydroxyl group of another

eg: hydroxyl group on C5 attacks carbonyl on C1

C5 bonds with oxygen from C1

Hydrogen is removed from C5 and added to C1’s oxygen, forming a new hydroxyl group

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simple sugar

mono or disaccharide

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oligosaccharide

made up of 3-10 sugar units

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complex sugar

made up of 3-1000 linked sugar units

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alpha linkages

bons between carbons from sugar groups that are below the rings

  • forms compact alpha helices and allows for branching, increasing energy storage

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beta linkages

bond between two carbons in sugar found above the rings

  • straight, parallel chains (formed by second sugar being flipped) allows for the formation of cross linkages that are formed by H bonds in adjacent strands, offering structural support

  • look at carbon to the left to determine type of linkage

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