Karteikarten
L6-Protein interacrtions
Karten in diesem Stapel (36)
- 1what is a small ligandany small molecule which can interact with a protein
- 2give some examples of ligandsneurotransmitters
other peptides
metal ions
metabolites - 3what interactions are normally formed between proteins and substratesnon covalent interactions
e.g ionic, hydrogen, hydrophobic, London - 4what is calmodulinreceptor of Ca2+ involved in membrane transport
- 5what is a multimeric proteinprotein made from multiple proteins containing Q structures
- 6what is the purpose of myosin and action filaments in myofibrilsslide past one and other to create muscle contraction
- 7comment on the fibrous and globular properties of myosincontains globular head and fibrous tail
- 8what is chromatinDNA strands wrapped around histones to form the nucleosome
- 9give some enzymes which interact with DNADNA helicase
restriction enzymes
transcription factors - 10what is a restriction enzymean enzyme which can cut across the DNA backbone
- 11do these proteins interact with the bases or the backbone of DNAbackbone
- 12give some protein lipid associationstransmembrane proteins
receptor proteins
(proteins embedded in the membrane) - 13whats the stages of proteins binding-recognition of complementary molecules
- association of the active site and complementary binding region - 14how does availability affect likelihood of bindingmore available substrates increases chance of collision between reactant molecules
- 15how does matching non-covalent interactions affect the likelihood and strength of bondingthe more complimentary the bonding between reactants the more likely it is that the reactants will be attracted and bind
- 16how does competition from inhibitors effect likelyhood of bindingdecreases likelihood as inhibitors can bind instead
- 17what decides the bonds which can be made by a proteins active sitethe primary sequence of amino acids and their R groups
- 18what amino acid is responsible for disulphide bridgescystine
- 19what different interactions can form between R groupsLondon forces
dipole interactions
ionic bonds
covalent bonds (disulphide) - 20what are protein domainsdifferent sections of the same protein which can form different interactions
- 21which is the strongest protein interactionionic
- 22what environmental change can alter ionic bondspH changes
- 23why does pH change affect ionic bondswill change the ionisation state of the R groups of ionically bonding proteins
- 24what 2 groups can be found on ionically binding R groupsNH2 groups and COOH groups
- 25give some examples of PTMmethylation
acetylation
phosphorylation - 26what charge does phosphate groups havenegative
- 27whats the effect of PTM's-changes the interactions which a protein can form
- can activate or inactivate proteins - 28how do different domains react to different PTM'sdifferent domains are specific to different PTM's
- 29what does different protein domains mean for specificitymeans a single protein can be specific to a number of different substrates
- 30which structural Level contributes to multiple domains the mostmultimeric protein levels
- 31what different substrates do polymerase enzymes need to interact withthe backbond
the bases
regulatory proteins - 32how are protein interactions involved ion cell signalling-receptor proteins bind to signalling molecules on cell membrane
-triggers cascade of events leading to further reactions - 33how can protein interactions be measuresdmeasuring the concentrations of reactants and or products in a sample of proteins over time
- 34what is the dissociation constant of a ligandthe affinity of a ligand for a protein binding site
- 35what does a low dissociation constant of a ligand mean for its affinityit has a high affinity for the protein
- 36when is the Kd value reachedwhen the ligand concentration is enough to achieve 50% dissociation with the protein
Informationen
- Beschreibung
- Year 1 CBB(c) Karteikarten am L6-Protein interacrtions , erstellt von Jack Rowe am 26/12/2021.
- Erstellt von
- Jack Rowe
- Aufrufe
- 2
- Bewertung