Topic 2 Flashcards
what is cystic fibrosis?
a genetic disorder in which abnormally thick and sticky mucus is produced in the lungs and other parts of the body.
what is the cause of cystic fibrosis?
a faulty recessive allele of the gene that codes for the transporter protein CFTR.
how is cystic fibrosis diagnosed?
- a sweat test (to measure the amount of salt in sweat which would be abnormally high in patients with CF).
- a genetic test (a sample of blood or saliva is tested for the faulty allele).
what are the properties of gas exchange surfaces in living organisms?
- LARGE SURFACE AREA TO VOLUME RATIO (large objects have a smaller surface area to volume ratio than small objects. the smaller the surface area to volume ratio the slower the rate of exchange).
- THICKNESS OF SURFACE (the rate of diffusion is inversely proportional to the thickness of the gas exchange surface. a thin surface provides a short diffusion pathway).
- DIFFERENCE IN CONCENTRATION (a steep gradient in oxygen and carbon dioxide concentration allows a faster rate of diffusion).
how can the rate of diffusion be calculated using Fick’s Law?
rate of diffusion is proportional to
surface area x difference in concentration / thickness of gas exchange surface.
- rate of diffusion is directly proportional to surface area.
- rate of diffusion is directly proportional to the difference in concentration across the gas exchange surface.
- rate of diffusion is inversely proportional to the thickness of the gas exchange surface.
how is the structure of the mammalian lung adapted for rapid gaseous exchange?
- THIN BARRIER TO REDUCE DIFFUSION DISTANCE: the alveolus epithelium is one cell thick, the capillary endothelium is one cell thick, the capillaries are in close contact with the alveolus walls.
- LARGE SURFACE AREA provided by lots of alveoli.
- A STEEP CONCENTRATION GRADIENT maintained by ventilation and blood flow.
- extensive capillary network around each alveoli provides large surface area for gas exchange.
what is the structure and properties of a cell surface membrane?
(phospholipid bilayer)
consists of a PHOSPHOLIPID BILAYER.
HYDROPHOBIC TAILS orientates itself away from water towards the centre of the membrane.
HYDROPHILIC HEADS orientates itself towards water.
lipid-soluble material moves through the membrane via the phospholipid portion.
water soluble substances are prevented from entering and leaving the cell.
the phospholipid bilayer makes the membrane FLEXIBLE and SELF SEALING.
what is the structure and properties of a cell surface membrane?
(proteins)
EXTRINSIC PROTIENS: located on the surface of the bilayer. act as mechanical support or in conjunction with glycolipids as cell receptors.
INTRINSIC PROTEINS: span the phospholipid bilayer. protein channels allow water soluble ions to diffuse across the membrane. carrier proteins bind to ions or molecules then change shape in order to move the molecule across the membrane.
what is the structure and properties of the cell surface membrane?
(cholesterol)
these molecules are hydrophobic.
prevent lateral movement.
make the membrane less fluid at higher temperatures.
prevent leakage of water and dissolved ions from the cell.
what is the structure and properties of the cell surface membrane?
(carbohydrate chains)
GLYCOLIPIDS: made up of carbohydrate chains covalently bonded with a lipid. act as recognition sites. maintain the stability of the membrane. help cells to attach to one another to form tissues.
GLYCOPROTEINS: carbohydrate chains attached to extrinsic proteins. act as recognition sites (hormones). help cells to attach to one another to form tissues. allows cells to recognise from one another e.g. lymphocytes.
describe the fluid mosaic model as an explanation of the structure and properties of the cell surface membrane.
FLUID: the individual phospholipid molecules can move relative to one another. this gives the membrane a flexible structure that is constantly changing shape.
MOSAIC: the proteins are embedded in the phospholipid bilayer and vary in shape, size and pattern.
what is osmosis?
the diffusion of free water molecules across a partially permeable membrane from an area of higher concentration of water molecules to an area of lower concentration of water molecules.
what is meant by passive transport?
no metabolic energy is required for it to happen.
the process is driven by the concentration gradient itself.
(diffusion and facilitated diffusion)
what is diffusion?
the net movement of particles from an area of higher concentration to an area of lower concentration.
particles diffuse down a concentration gradient.
what is facilitated diffusion?
diffusion through carrier proteins or channel proteins.
how are carrier proteins involved in membrane transport?
move large hydrophilic molecules into or out of a cell down a concentration gradient.
the ion or molecule binds onto a specific site on the protein.
the protein changes shape and as a result the ion or molecule crosses the membrane.
how are channel proteins involved in membrane transport?
polar molecules or ions diffuse through water filled pores within the channel protein.
each type of channel protein has a specific shape that permits the passage of only one type of ion or molecule.
some channel proteins can be opened or closed depending on the presence or absence of a signal e.g. a hormone (these channels are called gated channels).
describe active transport.
uses energy in the form of ATP to move molecules and ions across plasma membranes against a concentration gradient. this process involves carrier proteins.
ATP is produced by respiration and acts as an immediate source of energy in a cell.
when ATP is hydrolysed in the cell, energy is released.
describe endocyctosis.
some molecules are too large to be taken into a cell by carrier proteins.
a cell instead can surround a substance with a section of its cell membrane.
the membrane then pinches off to form a vesicle inside the cell containing the ingested substance.
this process also uses ATP for energy.
describe exocytosis.
some substances produced by the cell need to be released.
vesicles containing these substances pinch off sacs of the Golgi apparatus and move towards the cell membrane.
the vesicles fuse with the cell membrane and release their contents outside the cell.
this process uses ATP as an energy source.
describe: monomer dipeptide polypeptide protein
the monomer of proteins are AMINO ACIDS.
a dipeptide is formed when two amino acids join together.
a polypeptide is formed when more than two amino acids join together.
proteins are formed when one or more polypeptide chains fold into a specific shape that allows it to perform a specific function.
what is the general structure of an amino acid?
a central carbon (C) atom bonded to a carboxyl group (-COOH), an amine group (-NH2), a hydrogen atom (-H) and an R group (-R).
what varies between each amino acid?
the R group is different in each amino acid. it can vary by: size polarity charge
how is a dipeptide formed?
two amino acids are joined together by a CONDENSATION REACTION to form a dipeptide.
the condensation reaction occurs between the CARBOXYL GROUP (-COOH) and the AMINE GROUP (-NH2) on adjacent amino acids.
a molecule of water is released as one oxygen and two hydrogen atoms are removed from the amino acids.
this creates a PEPTIDE BOND.
what type of bond is a peptide bond?
a covalent bond formed when two amino acids are joined together in a condensation reaction.
how is a polypeptide formed?
many amino acids can be joined together in a series of CONDENSATION REACTIONS to form a polypeptide.
what is a polypeptide?
a POLYMER made of many amino acids joined together by PEPTIDE BONDS through a series of CONDENSATION REACTIONS.
what is meant by a buffer?
amino acids acts as a buffer ( a solution that resists pH change).
too acidic = to many H+ ions.
too alkali = not enough H+ or too many OH- ions.
what is meant by a hydrolysis reaction?
a dipeptide can be broken down into two amino acids through a hydrolysis reaction.
a hydrolysis reaction requires water as one oxygen and two hydrogen atoms are added to the dipeptide.
this breaks the peptide bond forming two amino acids.
polypeptides can be broken down into amino acids by a series of hydrolysis reactions.
what is meant by the primary structure of a protein?
the specific sequence of amino acids in the polypeptide.
describe the primary structure of protein.
when a polypeptide is formed, the order of amino acids determines the primary structure of a protein .
there are 20 different naturally occurring amino acids.
every protein has a unique primary structure therefore function.
what is meant by the term secondary structure of a protein?
the polypeptide chain folding into either an alpha helix or beta pleated sheet, held together by hydrogen bonds.
describe the secondary structure of a protein?
polypeptides can fold in two main ways:
alpha helix ( a coil)
beta pleated sheets (a zig-zag folded over itself)
all amino acids in the polypeptide chain contain a -C=O group and a -NH group when bonded.
the hydrogen in the -NH is slightly positive and the oxygen in the -C=O is slightly negative resulting in hydrogen bonds between the amino acids in the polypeptide chain.
are hydrogen bonds strong or weak?
hydrogen bonds are weak but the many hundreds of them keep the secondary structure stable.
what is meant by the term tertiary structure of a protein?
the specific interaction of folding into the specific 3D shape driven by the bonds formed between the R groups of the amino acids.
describe the different bonds formed between R groups in the tertiary structure.
HYDROGEN BONDS form between POLAR (delta positive and delta negative) R groups.
IONIC BONDS form between POSTIVE and NEGATIVELY charged R groups.
DISULPHATE BRIDGES form between SULPHUR atoms in R groups.
what else determines the 3D structure of the protein?
Amino acids with HYDROPHOBIC R groups tend to be found in the centre of the protein.
Amino acids with HYDROPHILIC R groups tend to be found on the outside of the protein.
all determine the specific 3D structure of a protein.
why are the properties of amino acid R groups so important?
the overall 3D structure of a protein is a result of properties and therefore interactions.
the primary structure determines the tertiary structure.
what is meant by the term the quaternary structure of a protein?
the specific 3D shape that is determined by the multiple polypeptide chains and/or prosthetic groups bonded together.