Topic 2 Flashcards
The rate of gas exchange by diffusion is increased by:
- surface area increase
- diffusion disatnce decrease
- diffusion concentration gradient made more steep
Fick’s law:
rate of diffusion (is proportional to) surface area x concentration difference / diffusion distance
How are mammalian lungs adapted for rapid gas exchange?
- large surface area due to the presence of many alveoili
- steep concentration gradient maintained due to good supply of circulating blood provided by the capillary network and mechanical ventilation
- short diffusion distance as the alveoli and capillaries are only one cell thick
5 functions of cell membrane:
- is flexible- can break and fuse easily
- compartmentalisation- e.g. lysosome controls cell death, phagocytosis
- partially permeable
- cell signalling- glycoproteins are antigens (cell recognition), glycolipids can send and recieve messages (e.g. a hormone receptor)
- site of cell reactions- have enzymes allowing reactions to take place
explain the term: fluid mosaic model:
fluid= components of the cell membrane are able to move freely laterally through the bilayer
mosaic= many different components making up the cell membrane e.g. phospholipids, proteins, cholesterol, carbohydrates etc.
Types of passive movement of molecules into and out of the cell:
- Diffusion- passive movement of small, non-polar molecules from an area of high concentration to low concentration (down a conc. grad.) The molecules move through the phospholipid bilayer.
- Facilitated diffusion- requires channel proteins to tranport small, polar molecules across the membrane.
- Osmosis- the movement of water molecules from an area of low solute concentrations to high solute concentrations through a partially permeable membrane.
Types of active movement of molecules into and out of the cell:
- active transport- can transport all types of molecules through carrier proteins. Movement may be up or down the concentration gradient. Up the gradient reaquires the hydrolysis of ATP to provide an accesible store of energy for biological processes. The phosphorelation (reforming of ATP) requires energy.
- Endo/exocytosis- transport large molecules. In endocytosis, particles are enclosed in vesicles made from the cell surface membrane and transported into the cell. In exocytosis, vesicles containing large particles are fused with the cell surface membrane and transported out of cells.
DNA structure:
- double stranded, alpha doubel helix with a sugar-phosphate backbone on each strand
DNA-
bases:
pairing:
sugar:
bases:
purine (two nitrogen-containing rings): adenine and guanine
pyrimidine (1 nitrogen-containing ring): cytosine and thymine
pairing: A-T, C-G
sugar: deoxyribose (hydroxy group replaced by hydrogen on carbon 2)
Bonding in DNA:
-Phosphodiester bonds between phosphate group and carbon 5 (and between adjacent nucleotides forming the sugar-phosphate backbone)
-Hydrogen bonds between bases (3 between G-C and 2 between A-T)
mRNA structure:
single stranded, not folded, carries codons (triplets of bases) which attach to tRNA via H bonds
mRNA-
bases:
pairing:
sugar:
bases:
purine: adenine and guanine
pyrimidine: cytosine and uracil (thymine is too unstable to leave the nucleus)
pairing: A-U, C-G
sugar: ribose
tRNA structure:
single stranded, folded into a specific pattern held together by H bonds, carries anticodons complementary to mRNA codons, bonded via H bonds.
Transcription process:
mRNA made in the nucleus:
1. DNA helicase unzips the DNA, breaking the H bonds between the complementary bases. The DNA uncoils, thus separating the two strands.
2. One of the DNA strands is used as a template to make the mRNA molecule. The template is called the antisense strand.
3. Free nucleotides line up by complementary base pairing and adjacent nucleotides are joined by phosphodiester bonds, thus forming a molecule of mRNA. This is catalysed by RNA polymerase.
4. mRNA moves out of the nucleus through a nuclear pore and attaches to a ribosome (in cytoplasm or RER) which is the site of protein synthesis
Translation process:
Amino acids join together to form a polypeptide chain:
1. mRNA attached to a ribosome, tRNA binds to specific amino acids from the cytoplasm depending on its anti-codon (activation)
2. complementary anticodons of tRNA bind to mRNA codons and are bonded with H bonds
3. The ribosome joins the amino acids attached to two tRNA molecules with a peptide bond and the tRNA molecules detach from the amino acids.
4. Process is repeated leading to the formation of a polypeptide chain until stop codon is reached on mRNA.
definition of a gene:
A gene is a sequence of bases on a section of DNA coding for a sequence of amino acids in a polypeptide chain.
names for non-coding and coding regions:
non-coding = introns
coding = exons (expressed)
3 features of the genetic code:
- the genetic code is non-overlapping- each triplet of bases is only read once and triplets don’t share any bases
- the genetic code is degenerate- more than one triplet codes for the same amino acid
- the genetic cose is a triplet code- each three bases codes for 1 amino acid. It also contains start and stop codons (starting or stopping protein synthesis)
Proteins: monomers
Amino acids:
-contains one amine group, a carboxyl group and a variable R group (carbon-containing chain). There are 20 different amino acids with different R groups.
- joined by peptide bonds formed in condensation reactions
Primary and secondary structure of proteins:
Proteins are folded in the Rough Endoplasmic Reticulum.
1. Primary structure of a protein is the sequence of amino acids, making up a polypeptide chain.
2. The secondary structure is the 2D arrangement of the chain of amino acids- either alpha helix or beta pleated sheet.
Tertiary and Quaternary structure of proteins:
- Tertiary structure of a protein is the 3D folding of the secondary structure into a complex shape. The shape is determined by the types of bonds present- -Hydorgen bonds (between partially charged atoms in R groups)
-ionic bonds (salt brigdes, form between oppositely charged groups on R groups)
-disulfide bridges (covalent bonds between sulfur atoms on cysteine)
- hydrophilic and hydrophobic interactions (polar and non-polar properties in R groups) - Quaternary structure of a protein is the 3D arrangement of more than one polypeptide chain.
Fibrous protein features:
- long, parallel polypeptides
- very little tertiary/ quaternary structures
-occasional cross-linkages which form microfibres for tensile strength
-insoluble
-used for structural purposes- such as collagen
Globular protein features:
-complex tertiary/ quaternary structures
-form colloids in water
-used for transport e.g. hormones, antibodies, carrier proetins (e.g. haemoglobin)
The fibrous proetin- collagen:
- High tensile strength due to presence of both hydrogen and covalent bionds.
-made up of three polypeptides which form an alpha triple helix which forms fibrils and strong collagen fibres.
-forms the structure of bones, cartilage and connective tissue, is the main component of tendons