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
Nucleotide components
base+ sugar+ phosphate [e.g. adenosine monophosphate (AMP)]
26
RNA
ribonucleic acid
27
DNA
deoxyribonucleic acid
28
Functions of nucleotides
1. short-term energy carriers (ATP) 2. storage and retrieval of biological information (DNA, RNA)
29
Macromolecules are the most
abundant of the organic molecules in a living cell
30
Examples of macromolecules
DNA, RNA, protein, polysaccharides
31
native state of a molecule (concept)
generally, all molecules of a given protein or RNA species adopt the same 3D conformation despite the countless folding possibilities!!!
32
which type of interactions specify the precise shape of the molecule (native state)
noncovalent interactions (electrostatic interactions, hydrogen bonds, van der waals attractions, hydrophobic interactions)
33
strong binding of macromolecules requires
-good specificity between macromolecules (the cumulative effect of many covalent bonds can be very strong but require multiple points of contact)
34
what interactions act as building blocks to form much larger structures?
noncovalent interactions
35
metabolic intermediates
the compounds formed along the pathways leading to the end product but have no real function
36
weak attractions between adjacent water molecules are
hydrogen bonds