lecture 3 Flashcards

1
Q

element

A

can’t be broken down
-single atom

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2
Q

atom

A

smallest particle of an element that still retains its properties

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3
Q

molecule

A

two or more atoms join together chemically

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4
Q

compound

A

molecule that contains at least two different elements

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5
Q

covalent bond

A

strong bonds formed by the sharing of electrons between adjacent atoms

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6
Q

bond strength/dissociation energy

A

amount of energy required to break a bond
-covalent= more energy needed to break

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7
Q

polar covalent bond

A

unequal sharing of electrons due to a difference in EN

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8
Q

non covalent interactions

A

bond that does not involve the sharing of electrons
-ex. the components of DNA (A and T, G and C)
-very weak, but cumulatively very stong!!!

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9
Q

Ionic bonds

A

results from the loss or gain of electrons

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10
Q

hydrogen bonds

A

very important in biochemistry!!!!

-covalently bonded H atom on a donor group interacts w a pair of non-bonded electrons on an acceptor group

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11
Q

Hydrogen acceptors are

A

electronegative atoms (generally N or O)

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12
Q

polar molecules surrounded by water can dissociate into

A

acid= releases protons
base= accepts a proton

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13
Q

macromolecule: nucleic acid

A

subunit: nucleotide

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14
Q

Macromolecule: triacylglycerol and membrane lipid

A

subunit: fatty acid

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15
Q

macromolecule: polysaccharide

A

subunit: sugar

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16
Q

macromolecule: protein

A

subunit: amino acid

17
Q

the simplest sugars are

A

monosaccharides

18
Q

monosaccharides can be joined through glycosidic bonds to form

A

disaccharides (two monomers together), oligosaccharides (2-10 monomers) or polysaccharides (more than 10 monomers)

19
Q

function of sugars (5)

A
  • energy source
    ex. glucose can be stored as glycogen
  • can be used for structure
    ex. cellulose forms cell walls
    ex. chitin found in the insect cytoskeletons
  • slime, mucus
    ex. Phlegm is sweet due to the oligosaccharide chains (glycans ) covalently attached to amino acid side-chains of the glycoproteins in phlegm
  • modification of proteins and lipids
  • information storage (ribose and deoxyribose in DNA)
20
Q

Fatty acids (FA) –> triacylglycerols (TAG) and membrane lipids

A

FAs for TAG which serve as an energy source

FAs form membrane lipids which contribute to membrane structure and function

21
Q

amino acids have the same basic structure with a

A

variable side chain

22
Q

polypeptides

A

long chains of amino acids

23
Q

how is the final 3D structure of a protein formed?

A

amino acids fold by using covalent and noncovalent interactions

24
Q

Nucleoside components

A

base+ sugar (e.g. adenosine)

25
Q

Nucleotide components

A

base+ sugar+ phosphate [e.g. adenosine monophosphate (AMP)]

26
Q

RNA

A

ribonucleic acid

27
Q

DNA

A

deoxyribonucleic acid

28
Q

Functions of nucleotides

A
  1. short-term energy carriers (ATP)
  2. storage and retrieval of biological information (DNA, RNA)
29
Q

Macromolecules are the most

A

abundant of the organic molecules in a living cell

30
Q

Examples of macromolecules

A

DNA, RNA, protein, polysaccharides

31
Q

native state of a molecule (concept)

A

generally, all molecules of a given protein or RNA species adopt the same 3D conformation despite the countless folding possibilities!!!

32
Q

which type of interactions specify the precise shape of the molecule (native state)

A

noncovalent interactions
(electrostatic interactions, hydrogen bonds, van der waals attractions, hydrophobic interactions)

33
Q

strong binding of macromolecules requires

A

-good specificity between macromolecules

(the cumulative effect of many covalent bonds can be very strong but require multiple points of contact)

34
Q

what interactions act as building blocks to form much larger structures?

A

noncovalent interactions

35
Q

metabolic intermediates

A

the compounds formed along the pathways leading to the end product but have no real function

36
Q

weak attractions between adjacent water molecules are

A

hydrogen bonds