Exam 1 Flashcards

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1
Q

hydrogen bond

A

If a partially charged oxygen
(negative) from one molecule is
interacting with a partially charged
hydrogen (positive) from another
molecule, what type of interaction is
happening

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2
Q

covalent bonds

A

non-polar- share electrons equally and hydrophobic
polar-share unequally and are hydrophilic

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3
Q

Non-covalent bonds provide what

A

flexibility

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4
Q

The protein interacts with the lipids in the plasma membrane:

A

hydrophobic

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5
Q

protein interacts with water in the cytoplasm

A

hydrogen bonds

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6
Q

Amino acid side chain interact with water as water flows through the channel:

A

hydrophilic

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7
Q

ionic bonds

A

-Made when on atom gives up an electron and creates negative and positive
-in cell not as strong as covalent bonds

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8
Q

CHONP

A

Carbon, hydrogen, oxygen, nitrogen, potassium/other

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9
Q

T/F: all monomers of macromolecules have directionality, so macromolecules have directionality

A

TRUE

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10
Q

Monomer activation (step 1)

A

addition of a monomer to a carrier molecule (uses ATP)

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11
Q

Which macromolecule uses ionic bonds for folding

A

proteins

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12
Q

Match monomers to each macromolecule

A

Protein: amino acid (peptide bonds)
Carbs: monosacs
Nucleic acids: nucleotides (phospho)
Lipids: fatty acids

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13
Q

step 2 of macro synthesis

A

condensation/dehydration reaction between two monomers

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14
Q

step 3 macro synthesis

A

repeated condensation reactions to make polymer

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14
Q

Nucleotides include

A

pyrimidines (1 ring): Uricil, cytosine, thymine
Purine (2 ring): Adenine and guanine

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15
Q

Acidic or negative side chains

A

aspartic and glutamic acid

16
Q

basic side chains or positive

A

lysine, arginine and histidine

17
Q

uncharged polar side chains

A

Asparagine, glutamine, serine, threonine, tyrosine

18
Q

Non-polar side chains

A

Alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan, glycine, and cysteine

19
Q

Assemblers for each macromolecule

A

Protein: ribosome (ionic interactions, hydrogen bonds, hydrophobic interaction)
Nucleic acid: polymerases (H bonds)
Polysaccs: glycosyl transferases
Lipids: fatty acid synthases (hydrophobic)

20
Q

protein function is limited and defined by what

A

protein structure

21
Q

4 levels of protein structures

A

primary (covalent bonds)
secondary (between amine and carbonyl groups from backbones)
tertiary
quaternary

22
Q

Transmembrane proteins

A

go all the way through the membrane

23
Q

monolayer associated

A

go only in half the lipid membrane

24
Q

lipid-linked-

A

interact with attached lipid and hydrophobic membrane

25
Q

protien attached

A

associated with a protein that is associated with the cell

26
Q

Cholesterol

A

cold makes membrane more fluid, but hot makes membrane more ridgid

27
Q

Membranes are fluid

A

held together non-covalently, bonds can be easily broken and created

28
Q

Amphipathic

A

hydrophilic and hydrophobic

29
Q

Saturated membranes

A

long chains more rigid, more hydrophobic interactions

30
Q

unsaturated membrane

A

shorter, decrease distance in the kinks, more rigid

31
Q

What molecules can just cross a membrane?

A

small, nonpolar molecules

32
Q

simple diffusion

A

when molecules cross with their concentration gradient and without energy

33
Q

Facilitated diffusion

A

Channel- mediated: very specfic holes
transporter mediated: use allostery and is saturatable

34
Q
A