Exam 1 Flashcards

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
lipid-linked-
interact with attached lipid and hydrophobic membrane
25
protien attached
associated with a protein that is associated with the cell
26
Cholesterol
cold makes membrane more fluid, but hot makes membrane more ridgid
27
Membranes are fluid
held together non-covalently, bonds can be easily broken and created
28
Amphipathic
hydrophilic and hydrophobic
29
Saturated membranes
long chains more rigid, more hydrophobic interactions
30
unsaturated membrane
shorter, decrease distance in the kinks, more rigid
31
What molecules can just cross a membrane?
small, nonpolar molecules
32
simple diffusion
when molecules cross with their concentration gradient and without energy
33
Facilitated diffusion
Channel- mediated: very specfic holes transporter mediated: use allostery and is saturatable
34