Unit 1 Flashcards
(129 cards)
proteome
all the proteins expressed by a genome
why is the proteome larger than the number of genes?
alternative RNA splicing and post-translational modification
amino acid link
peptide bonds
primary structure
the sequence in which amino acids are synthesised into the polypeptide
types of secondary structure
alpha helixes, parallel or anti-parallel beta sheets, turns
what holds together the secondary structure?
hydrogen bonding in the backbone of the protein strand
classes of R groups
- positively charged (amine nh2)
- negatively charged (carboxyl)
- polar (hydroxyl)
- hydrophobic (hydrocarbon)
ligand
substance that can bind to proteins
what happens when a ligand binds to a protein binding site or when a substrate binds to an
enzyme’s active site?
the conformation of the protein changes which causes a functional change
prosthetic group
non-protein unit bound tightly to a protein which is necessary for its function
what can interations of R groups be influenced by?
temperature and pH
possible interactions in tertiary structure
hydrophobic interactions, ionic bonds, hydrogen bonds
in which proteins can quartenary structure exist?
proteins with several connected polypeptide subunits
in archaea, how do bacteriorhodopsin molecules generate potential differences?
by absorbing light to pump protons across the membrane and the resulting
diffusion of hydrogen ions back across the membrane drives ATP synthase.
In plants, what does the light absorbed by photosynthetic pigments within protein
systems do?
drives an electron flow that pumps hydrogen ions across the thylakoid membrane of the chloroplast and the resulting diffusion of hydrogen ions back across the membrane drives ATP synthase
what forms rhodopsin?
opsin and retinal
what does different forms of opsin do in cone cells?
give sensitivity to specific wavelengths of light (red, green, blue or UV)
what does rhodopsin and the protein cascade do in rod cells?
absorbs a wider range of wavelengths, and a
greater degree of amplification by the protein cascade results in sensitivity at low light intensities
what amplifies light signals in eyes?
a cascade of proteins
Process of a nerve impuulse being generated once rhodopsin is excited by a photon of light
Excited rhodopsin activates G-proteins
which activate many enzyme molecules. The enzyme molecules cause the closure of ion channels by catalysing the removal of molecules that keep channels open. The inward leakage of positive ions is halted so the membrane potential increases. Hyperpolarisation (increasing charge) stimulates a nerve impulse.
what are membranes made of?
a bilayer of phospholipid molecules and a
patchwork of protein molecules.
where are hydrophyllic R groups in a protein?
surface of a soluble protein found in the cytoplasm
where are hydrophobic R groups in a protein?
they cluster at the centre of a protein to form a globular structure
peripheral proteins
- proteins that temporarily attach to the cell membrane
- have less hydrophobic R groups interacting with phospholipids