Sections I-IV Vocab Flashcards

1
Q

hydrogen bonds

A

a hydrogen atom covalently bound to one electronegative atom also attracted to another electronegative atom

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Electronegativity

A

elements that differ in their affinity for electrons. Share electrons unequally

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Hydrophilic

A

form weak bonds to water molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Synthesis

A

A reaction that increases the structural complexity. An example is polymerization.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Polymerization

A

A large subset of group reactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Condensation-Dehydration

A

Two molecules combine and small molecules are lost

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Hydrolysis

A

Breakdown of an organic molecule by adding water H2O.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Polysaccharides

A

100 to 1000 monosaccharides linked together

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Triglyceride

A

Three fatty acids linked to a glycerol molecule. Energy storage (fat),

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Phospholipid

A

Principal component of cell membranes. Two fatty acids and a polar head group.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Peptide bond

A

amino groups joined together. the alpha amino group of one amino acid and alpha carboxyl group of a second.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Primary structure

A

Sequence of amino acids in its polypeptide chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Secondary structure

A

Regular arrangement of amino acids. Localized regions of polypeptide: alpha helix and beta sheets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Alpha helix

A

region of polypeptide chain coils itself, with the CO group of one peptide forming an h-bond with NH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Beta sheets

A

two parts of a polypeptide chain lie side by side with hydrogen bonds between them

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Tertiary structure

A

Folding of a single polypeptide. Interaction of the side chains of amino acids that live in different regions of the primary sequence. Structures are called domains. Localization of hydrophobic AA’s in the interior of the protein and the hydrophilic amino acids on the surface

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Quaternary structure

A

Interactions between polypeptide chains in proteins composed of more than one polypeptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Oxidation

A

loss of electron density, loss of oxygen or hydrogen

19
Q

Reduction

A

gain of electron density, happens usually by gaining a hydrogen

20
Q

Free energy

A

changes in enthalpy and entropy. Predicts whether or not the rxn is energetically favorable.

21
Q

Activation energy

A

The energy required to reach the transition state. Role of an enzyme is to lower the activation energy by having multiple reactants come together.

22
Q

Allosteric modification

A

“other site”. enzyme activity is controlled by binding small molecules to regulatory sites on the enzyme. Consists of multiple subunits and worlds directly on the affected protein and is faster.

23
Q

Covalent modification

A

Needs to make the object before, turns it on and phosphorylates it. Longer lasting and less prone to fluctuation

24
Q

Peripheral (Extrinsic) Membrane

A

Proteins that dissociate from the membrane following treatments with polar reagents, such as pH or high salt concentrations. Soluble in aqueous solutions.

25
Integral (Intrinsic) Membrane
Inserted into the lipid bilayer. Only broken down if the membrane is broken down by detergents.
26
Fluid (Fluid Mosaic Model)
membrane held together mainly by hydrophobic interactions lipids and some proteins can drift laterally
27
Mosaic (Fluid Mosaic Model)
Membrane is a collage of different embedded proteins
28
Passive Diffusion
A molecule simply dissolves in the phospholipid bilayer, diffuses across it, and then dissolves in the aqueous solution on the other side. No energy is needed
29
Facilitated Diffusion
Involves the movement of molecules in the direction determined by their relative concentrations inside and outside of the cell. No energy is needed. Ex - carrier proteins and channel proteins
30
Active Transport
Energy is provided for maintaining gradients of ions across the plasma membrane. Example: Na+ - K+ pump
31
Cotransport
type of secondary active transport; gradient established by Na+-K+ pump (animal cells). transports of other molecules coupled to movement down these gradients. Symport and Antiport.
32
Channel
Form open pores in the membrane that allow small molecules of the appropriate size and charge to pass freely through the bilayer. They allow gases, hydrophobic molecules, small uncharged polar
33
Carriers
Bind specific molecules to be transported on one side of the membrane. Undergo conformational changes that allow the molecules to pass through
34
Pumps
Responsible for maintaining the gradients of ions across the plasma membrane provides
35
Glycosaminoglycan (GAGs)
Hydrated gel due to the negative charge on the outside attracting positive ion molecules which attracts water. Resists compression forces.
36
Proteoglycans
proteins and GAGs linked together. Creates hydrated gels in plant cells. Provides hydrated space and forms gels of varying pore size and charge density.
37
Collagen
Rich in proline and glycine residues. Resists tensile forces.
38
Elastin
Vertebrae tissues such as skin, blood vessels, and lungs. Needs to be both strong and elastic in order to function
39
Fibronectin
Prototype adhesion proteins in all vertebrae
40
Nuclear pore complex
Only channels through which small polar molecules, ions, and macromolecules (proteins, RNA) can go through. Composed of about 30 different pore proteins (nucleoporins). Molecules travel through by freely diffusing and facilitated diffusion
41
NLS
Most often 1 or 2 short sequence rich in basic amino acids lysine and arginine
42
Importin
Nuclear localization signals are recognized by nuclear transport receptors. Carries the proteins into the nucleus; regulated by Ran. Activity is regulated by GTP binding and hydrolysis
43
Constitutive Secretion
All cells do this type of secretion. Happens a lot/ all the time. Secretion is constant
44
Regulated Secretion
Regulated when it happens. Only secreted when it is needed