Biophysics 2

Front 1

Describe two features of an atom.

Back 1

It is the smallest unit into which matter can be divided without the release of electrically charged particles.

The smallest unit of matter that has the characteristic properties of a chemical element. (elementary particle)

Front 2

Name the positively charged part of the atom? What subatomic particles reside within this.

Back 2

Nucleus

Proton and neutron.

Front 3

Name the subatomic particle which moves around in shells.

Back 3

Electron

Front 4

When the substances in a covalent bond have equal affinity for electrons it is called?

Back 4

Non-Polar

Front 5

Define polar and name the two domains.

Back 5

when one nucleus has a higher affinity for the shared electrons in a covalent bond and the electrons are distributed unevenly.

They have positive and negative domains.

Front 6

What is electrostatic interaction?

Back 6

When ionic substances are attracted by oppositely charged domains of polar substances.

Front 7

Name and explain the two principals of diffusion.

Back 7

Brownians Motion

A dissolved molecule or small particle suspended in fluid is constantly struck at random by molecules of the fluid in its neighbourhood as a result of which it wanders erratically.

Ficks Law

The random wandering causes an average drift from regions where they are denser to regions where they are rarer and the mean drift rate is proportional to the gradient of density.

Front 8

Name the two parts of the biological membrane and say which is polar/nonpolar and which is hydrophylic/hydrophobic.

Back 8

Head - polar - hydrophilic

Tails - nonpolar - hydrophobic

Front 9

What is a biological membrane

Back 9

A very thin boundary that both separates and links the living cells with the external environment. It permits cellular function by regulating transport, flow of information, nutrients and metabolites.

Front 10

Name four components of the memebrane

Back 10

channel proteins

surface proteins

trans membrane proteins

receptor rafts

Front 11

Name the three types of membrane transport

Back 11

Passive transport

Facilitated transport

Active transport

Front 12

Name the three types of passive transport

Back 12

diffusion

osmosis

dialysis

Front 13

Name the three types of facilitated transport

Back 13

Uniport

Symport

Antiport

Front 14

Define diffusion

Back 14

Process resulting from the random motion of molecules by which there is a net flow of matter from a region of high concentration to low concentration.

-Down a concentration gradient

Front 15

When is diffusion unreliable

Back 15

over long distances

Front 16

what is diffusion through a semipermiable membrane called

Back 16

osmosis

Front 17

What is oncotic pressure?

Back 17

form of osmotic pressure exerted by proteins.

Front 18

Compare the freshwater teleost and the marine teleost?

Back 18

Skin

Freshwater - the water diffuses in through the skin and ions diffuse out through the skin.

Marine - Ions diffuse in through the skin while water diffuses out.

Gills

Freshwater - actively uptake ions. Diffusion of water in through the gills and ions out through the gills.

Marine - active secretion of ions. Diffusion of ions in through the gills and water out through the gills.

Dialysis

Freshwater - Dilute urine with a mix of water and ions.

Marine - concentrated urine of ions and water.

Front 19

Define dialysis

Back 19

Separation of suspended colloidal particles from dissolved ions or molecules of small dimensions by means of their unequal rates of diffusion through the pores of a semipermiable membrane.

Front 20

Give an example of dialysis

Back 20

glomerular filtration

Front 21

is Uniport transport up or down a concentration gradient

Back 21

down

Front 22

give two examples of uniport

Back 22

aquaporin

potassium channels

Front 23

Give another name for symport

Back 23

Co-transport

Front 24

Is symport up or down the concentration gradient

Back 24

down

Front 25

How does symport work?

Back 25

two substrates normally an ion and a molecule must bind simultaneously to the same side of the transporter. There is conformational change and conductivity and both substrates are transported together.

Front 26

Give an example of Symport

Back 26

Absorption of sugars and amino acids.

Absorbed by enterocytes by cotrasport with sodium ions.

Front 27

Is Antiport up or down the concentration gradient?

Back 27

Down

Front 28

Define Antiport

Back 28

Two substrates, normally an ion and a molecule bind to opposite sides of the transporter before its conformational change and conductivity. One substrate is absorbed and the other secreted.

Front 29

Give an example of antiport

Back 29

Sodium-proton exchanger in the proximal convoluted tube of the kidneys.

Front 30

What is the function of active transport?

Back 30

To accumulate a high concentration of molecules that the cell needs such as ions, glucose, amino acids.

It is against the concentration gradient.

Front 31

Name the two types of active transport and give an example of each.

Back 31

Primary active transport - Na-K ion pump

Secondary active transport - Symport/Antiport

Front 32

Name the type of active transport which uses high energy phosphage bonds.

Back 32

Primary active transport - Na-K pump

Front 33

Name the type of active transport that uses electrochemical gradient.

Back 33

secondary active transport - Symport/Antiport

Front 34

Define electrochemical gradient.

Back 34

a spatial variation of both electrical potential and chemical concentration across a membrane resulting in a type of potential energy available for work in a cell.

Front 35

How do proteins work?

Back 35

They change the structural organisation or shape of their subunits.

Front 36

Name two types of proteins and give an example of each.

Back 36

Dynamic proteins - enzymes/membrane channels

Strucutral proteins - Actin filaments, B-Keratin

Front 37

What state do proteins tend to maintain?

Back 37

The lowest possible energy state

Front 38

Where does energy shaping of protein come from?

Back 38

interactions between its components (from subunit to amino acid to atoms) and interactions with surrounding water molecules.

Front 39

Where do dynamic proteins get sufficient energy for a change of shape or structure?

Back 39

interactions with other substances