Cell Chemistry Flashcards

1
Q

Electrostatic forces between protons and electrons of two different atoms that hold them together

A

Chemical Bond

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2
Q

Holds atoms in the same molecule together

A

Intramolecular bonds

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3
Q

Bond that forms between two different molecules

A

Intermolecular bond

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4
Q

Bond formed by the attraction of oppositely charged ions through the loos or gain of electrons

A

Ionic bond

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5
Q

Bond between two atoms where the electrons are shared

A

Covalent bond

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6
Q

Allows rotation

A

Single Covalent bond

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7
Q

Allows bending

A

Double Covalent bond

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8
Q

No movement allowed

A

Triple Covalent bond

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9
Q

The force of attraction between a nucleus and electrons around it

A

Electronegativity

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10
Q

Electrons are shared equally in blank and occurs in atoms with similar or identical blank

A

nonpolar molecules, electronegativity

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11
Q

Electrons are shared unequally in blank and occurs in atoms with uneven blank

A

polar molecules, electronegativity

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12
Q

Water soluble

A

Hydrophillic

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13
Q

Not water soluble

A

Hydrophobic

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14
Q

Hydrophobic molecules

A

Ionic and non polar

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15
Q

Hydrophillic molecules

A

Polar

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16
Q

Part hydrophillic and part hydrophobic

A

Amphipathic

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17
Q

Building blocks of larger molecules

A

Monomers

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18
Q

Large molecules

A

Macromolecules

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19
Q

Molecules composed of covalently bonded monomers

A

Polymers

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20
Q

Weak bond formed between positive hydrogen and a more electronegative atom

A

Hydrogen bond

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21
Q

Weak bond that forms when nonpolar molecules associate tightly in a polar solvent

A

Hydrophobic interactions

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22
Q

Roles of hydrophobic interactions

A

Enzyme binding substrates, protein conformation, and stabilizing of RNA and cell membranes

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23
Q

Weak attractive force that occurs between molecules that are close together due to their polarity

A

Van der Waals forces

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24
Q

Characteristics of water

A

Polar, high specific heat, good solvent, and cohesive

25
Q

Ionic compound consisting of a cation and an anion held together by an ionic bond

A

Salts

26
Q

Proton donors, increase the concentration of H+ in a solution

A

Acids

27
Q

Proton acceptor, decrease the concentration oh H+ in a solution

A

Base

28
Q

Compounds that resist changes in pH by acting either as a acid or base

A

Buffers

29
Q

Polymers of amino acids and the most abundant macromolecule in cells

A

Proteins

30
Q

Polymers of nucleotides

A

Nucleic acids

31
Q

The two forms of nucleic acids

A

RNA and DNA

32
Q

Structural backbone of nucleic acids

A

Pentose

33
Q

Covalent bonds linking sugars together in a polysaccharide

A

Glycosidic bonds

34
Q

Polysaccharide composed of glucose monosaccharides joined by alpha glycosidic bonds

A

Starch

35
Q

Polysaccharide composed of glucose monosaccharides joined by beta glycosidic bonds

A

Structural polysaccharide

36
Q

Blank and blank are examples of structural polysaccharides

A

Cellulose and chitin

37
Q

Polysaccharide+protein

A

Gylcoprotein

38
Q

Polysaccharide+lipid

A

Glycolipid

39
Q

Cell surface receptors

A

Glycoproteins

40
Q

Important in cell walls of gram-negative bacteria

A

Glycolipids

41
Q

Three fatty acids bonded to a glycerol

A

Simple lipid

42
Q

No double bonds between carbons

A

Saturated fatty acid

43
Q

Double bonds between carbons

A

Unsaturated fatty acid

44
Q

Nitrogen base bonded to C5 sugar

A

Nucleoside

45
Q

Nitrogen base attached to C5 sugar by N-glycosidic linkage and bonded to phosphate

A

Nucleotide

46
Q

Purine Bases

A

Guanine and adenine, two heterocyclic rings

47
Q

Pyrimidine Bases

A

Thymine, cytosine, uracil, single heterocyclic ring

48
Q

DNA is held together by blank bonds

A

Hydrogen

49
Q

Amino acids are held together by blank bonds

A

Peptide

50
Q

Related but not identical molecules

A

Isomers

51
Q

Mirror image isomers

A

Enantiomers

52
Q

Enzymes capable of interconverting specific enantiomers

A

Racemases

53
Q

Catalytic proteins

A

Enzymes

54
Q

Linear arryay of amino acids in a polypeptide

A

Primary structure

55
Q

Folds in polypeptide that form a stable stucture consisting of hydrogen bonds

A

Secondary structure

56
Q

Additional folding of polypeptide giving greater stability and a 3-D shape

A

Tertiary Structure

57
Q

Occurs in proteins containing two or more polypeptides

A

Quaternary Structure

58
Q

Unfolding of polypeptide chain

A

Denaturation

59
Q

3 things that can cause denaturation

A

pH, temperature, and chemicals