Cells and Enzymes Flashcards
State the definition for a cell.
Cells are the fundamental unit of all living things on earth. They take nutrients and free energy from their surroundings and make copies of themselves.
Cells normally range between 1– 100µm in diameter.
What are universal features of all cells on Earth?
1) All cells have a plasma membrane, usually a phospholipid bilayer.
2) All cells exchange molecules w surroundings
3) Cells communicate w receptor, intracellular signalling and effector proteins.
4) All cells store hereditary genetic info as DNA
5) Protein synthesis: Cells translate RNA into protein in the same way
6) Cells have universal organelles, compartmentalisation.
7) Life as a ‘pattern in flux’: molecules are constantly being replaced.
8) Evolution from common ancestor, grouped into 3 domains
Describe the three levels of homeostasis.
Chemical: molecules in cells or blood (biochemistry)
Cellular: maintenance of subcellular structures; proper distribution of organelle-specific proteins, lipids etc (cell biology)
Systemic: BP, water balance, food intake, body temp and energy storage etc (physiology)
Describe and explain the structure of DNA
DNA is 2 antiparallel polynucleotide chains coiled into a double helix, held by H bonds between AT and CG pairs. ACGT is the coding element of the DNA.
Each nucleotide has a nitrogenous base, phosphate group and deoxyribose sugar. Phosphodiester bonds hold the phosphate and sugar backbone.
Phosphate bonded to 3C on one side, and 5C on the other to form a 3, 5 phosphodiester linkage. DNA structure runs 5’ to 3’
Phosphate and deoxyribose sugar are constant, meaning they dont change. One complete turn= 10 base pairs
Complementarity of DNA strands helps repair and replication
In the structure of DNA, what are the 2 types of nitrogenous bases?
Purines and Pyrimidines.
Purines= 2 nitrogen containing rings. A and G are purines.
Pyrimidines= 1 nitrogen containing ring, T and C.
The bases pair by H bonding, purine to pyrimidine.
CG bond is stronger as it makes 3 H bonds (bond length 1.08nm). AT bond is weaker as it makes 2 H bonds (bond length 1.11nm)
Draw the basic structure of an amino acid, followed by its structure at different pH levels
Name the four principal groups of amino acid side chains
Amino acids can be polar or nonpolar.
Within polar amino acids, they can be + charged, - charged or uncharged
draw the formation of a peptide bond by condensation.
The left side is the amino terminal end and the right side is the carboxyl terminal end
The sequence of aa.s= primary structure of a protein
What are Beta pleated sheets?
Beta pleated sheets: Part of the secondary structure. Different parts of a protein oreintate themself in parallel or antiparallel. This is stabilised by H bonds entre adj strands
Parallel means that the N and C groups are the same on one side
Antiparallel means the N and C groups alternate (see image)
The side chains (see purple) of the a.a point to opp sides of the sheet.
Fibroin is a key example
What is alpha helix?
A secondary structure
H Bonds are formed between peptide bonds within a single strand of protein. Side chains protrude from sides of the helix. Sometimes residues are hydrophilic on one side of the helix and hydrophobic on the other.
Describe the tertiary structure
Helices and sheets are folded up into more densely packed globular structures.
The structures are stabilized by cv disulfide bonds entre cysteine residues.
Some enzymes need additional chemical components, or cofactors to form the completed holoenzyme. A holoenzyme contains both the pp chain and cofactor.
Apoenzyme + Cofactor —> Holoenzyme
What is the Quaternary structure?
Haemoglobin has 4 polypeptides + 4 heme groups
When 2 pp chains are bonded juntos. The same bonds in tertiary structure hold the subunits juntos.
describe the noncovalent interactions in proteins.
Non-covalent Interactions in Proteins:
H Bonds between neutral groups and peptide groups.
Ionic attraction between + and - side chains. Ionic repulsion between like charges on different chains.
Hydrophobic interactions bring hydophobic side chains into close proximity to push them away from aqueous surfaces
VDWs forces occur between any atoms close to each other
Can proteins form covalent interactions?
Proteins can also form covalent interactions to stabilise tertiary and quaternary structures. This is formed between Cys residues, where an oxidation reaction forms a disulphide bond.
This may crosslink a single pp chain (3° structure) or 2 separate molecules (4° Structure)
Describe and explain the shape of various protein types.
Water soluble proteins are often globular: hydrophilic residues mostly on the outer surface, hydrophobic residues in the protein. May assemble into filaments (actin) or tubes (e.g. tubulin).
In membrane proteins, hay externally located hydrophobic residues that interact w the membrane lipids. May have hydrophilic central channels.
Fibrous proteins like collagen have a triple helix (NOT alpha helix). Collagen molecules may assemble into long fibres or sheets. Other fibrous proteins=myosin and keratin.
describe the mutation leads to sickle cell anaemia.
Sickle-cell anaemia is caused by a point mutation on a beta Hb chain: Glu (negative) is replaced by Val (hydrophobic ) at position 6.
In the deoxygenated state, the mutant (HbS) molecules stick juntos and form insoluble fibres.
Precipitation of the major protein in the cell distorts the normal disc shape to the characteristic “sickle shape” and blocks capillaries. The fragile cells break⇢ anaemia.
Explain DNA replication
It is making more DNA.
DNA is unzipped.
Strands separate and each strand acts as a template.
Free nucleotides line up against comp base pairs.
DNA polymerase joins new nucleotides together.
DNA ligase joins DNA to form two identical double strands of DNA.
Each one consists of one new strand and one original strand.
This is semi conservative replication
What is the difference between DNA and RNA?
RNA is: single-stranded, has ribose instead of deoxyribose and U instead of T. Hay diff types of RNA in mammalian cells. Only mRNA encodes proteins
Outline the roles of mRNA, rRNA and tRNA
mRNA: codes for proteins
rRNA: form the basic structure of the ribosome and catalyse protein synthesis
tRNA: central to ps as adaptors between mRNA and aa.
Give the stop and start codons
Start: AUG
Stop: UAA, UAG UGA,
Also hay 3 reading frames in mRNA
Each frame translates a completely different peptide. Only 1 frame is used for each mRNA, determined by AUG start codon position.
Describe tRNA molecules
tRNA is attached to aa.s in a cv bond. The anti codon makes contact with the mRNA by recognising its triplet codon via comp base pairing.
Which antibiotics affect ps?
eg. tet binds to 30S and prevents tRNA binding
Chloramphenicol binds to 50S and blocks peptide bond formation
Limitations of Antibiotics Acting on Protein Synthesis?
- No action on viruses, which use the host’s protein synthesis machinery
- Resistance
May inhibit ps in mammalian mitochondria, which have ribosomes like bacteria
How do newly formed proteins know where to go?
For every organelle in the cell hay a specific class of signal sequence that determine where the new protein goes. These signal sequences bind to receptors which then mediates the import of the protein into the correct organelles
Draw and describe the nuclear pore complex.
The nuclear pore complex:
About 30 different proteins
500-1000 protein molecules
3000 to 4000 NPCs per mammalian cell
Mass: ~ 125 million daltons
How does the size of the protein molecule influence nuclear import?
For small protein molecules < 60 kDa, diffusion is sufficient for nuclear import
For larger protein molecules > 60 kDa, diffusion is not sufficient for nuclear import, and active transport is needed
How are larger proteins imported into the nucleus?
Nuclear proteins are recognised by a nuclear import receptor. The proteins that make up this receptor are called impartins.
The complex is formed by a cargo protein and a receptor. The import receptor facilitates transport of the protein across the nuclear envelope through the nuclear pores.
Once this complex reaches the nuclear lumen, the cargo protein is replaced by a Ran-GTP protein. This releases the cargo protein, the cargo is delivered to the nucleus.
Ran-GTP converts to Ran-GDP, meaning ya no puede bind to the import receptor, so its free. This import receptor goes back to the cytoplasm to bind to a new cargo.
State the roles of mitochondria.
Respiration, ATP synthesis
Heat generation(in brown fat)
Fatty acid metabolism
Intermediary metabolism (synthesis & breakdown of biomolecules)
What are the 2 ways in which proteins end up in mitochondria?
Proteins are imported from the cytoplasm into mitochondria but mitochondria has its own DNA, which makes some of its proteins inside the organelle.
Describe protein import into the matrix of Mitochondria
The signal sequence is recognised by a TOM receptor complex in the outer membrane of mitochondria.
The protein binds to the Tom complex, is handed over to a channel in the outer membrane, and moves into the inter membrane space.
When this occurs, the protein makes contact w an inner membrane Tim23 complex and moves into the matrix. The original signal sequence is cleaved off by signal peptidases. The mature protein reaches its destination.
Describe Insertion of Proteins into the Inner Mitochondrial Membrane
The signal sequence binds w the Tom complex receptor, enters the channel of the Tom complex, and then binds w the Tom complex on the inner membrane. Once the signal sequence reaches the matrix it is cleaved off.
A section of protein exits the Tim channel laterally and enters the membrane bilayer. The rest of the protein exits the Tom complex. You now have the mature protein w a transmembrane domain anchoring it in the inner membrane.