Study Guides (248,269)
Canada (121,449)
Biology (1,267)
BIO1140 (245)

Bio1140 - Pop Quiz - Questions + Answers.pdf

1 Page
Unlock Document

Kathleen Gilmour

Simple diffusion - molecule can move through the membrane on its own Passive transport - some sort of transport protein is required Integral membrane protein - general term for a class of proteins imbedded inside a membrane Channel protein - a specific type of integral membrane protein that creates a hole/channel/pore in the membrane to allow highly selective molecules to pass Channel - forms a space for the molecule to move through the membrane Carrier - molecule binds to the carrier in order to be transported through the membrane Primary active transport - pumps molecules against their diffusion gradient Secondary active transport - gradient created by the primary transport uses transport of a molecule down its gradient in order to carry another molecule through, against its diffusion gradient pump involves 2 separate transport proteins instead of one energy required is one step away from the molecule of interest that is to be carried against its gradient Jan 27th What is signal tranduction and why is it significant? What is it - process of converting chemical messenger into cellular response Significance - in the abscence of a signal transduction pathway the cell cannot respond to the signal Distinguish between a protein kinase and receptor tyrosine kinase. Protein kinase - general type of enzyme that transfers a phosphate group from atp to an amino acid residue within a protein Receptor Tyrosine kinase - specific kinase, also receptor, kinase activity is turned on when it is activated, it becomes capable of transfering inorganic phosphate to another protein, tyrosine transfers phosphates to tyrosine residues Discuss structure/function relationships for G proteins. What is the function of G proteins? linked to g protein couppled receptors, acts as a switch to turn on and off signal transduction pathways (turns things on or off in the cell) List structural features of G proteins 3 diff subunits, alpha beta gamma, activated = alpha and beta-gamma complex split from each other, found attached to inner side of membrane by fatty acid subunits alpha can bind GTP or GDP, it contains GTPase activity Relate structural features to function of G proteins for it to function as a molecular switch the alpha subunit need to have GTP bind to it in order for it to split into its two subunits linked to membrane = close to g protein coupling receptors, can move around in membrane alpha subunit can hydrolyze GTP and turn off the g protein not active = GDP active = GTP Jan 30th Contrast and compare the structure and function of a G coupled-coupled receptor and a receptor for a lipid-soluble signal (such as a steroid hormone) 1 receptor is on the membrane activated by water soluble signals which are prevented from entering the cell by the membrane the other is in the cell They share a ligand binding site 7 transmembrane domains Receptor for a lipid soluble compound binds to DNA due to its structural feature - DNA binding domain - allows it to regulate gene transcription - allows it to act as a transcription factor G-protein coupled receptor has a G protein domain Relate the structure of ATP to its function as the energy currency of the cell there are 3 phosphate groups on ATP carries negative charge when you split phosphate group off ATP you release energy that was put in to bind the two negative phosphates together in the first place phosphate is more stable independently whereas when it is bound to ATP = less stable since electrons cant distribute evenly over the entire atom Feb 3rd What is differential centriguation and why does it matter? a process of a sequence of steps that take advantage of the diff precipitation speeds of diff components due to their size, mass, and density to isolate specific cellular components Distinguish between allosteric regulation and covalent regulation. allosteric a compound that binds to the enzyme not at the active site but at another site and affects the activity of the enzyme increasing or decreasing it binds to enzyme non-covalently ~ like a temporary key and lock attachment covalent pyruvate dehydrogenase is an enzyme that can covalently regulate it covalent attachment/detachment modulates the activity phosphorylation is an exmaple covalent group is attached to the enzyme
More Less

Related notes for BIO1140

Log In


Join OneClass

Access over 10 million pages of study
documents for 1.3 million courses.

Sign up

Join to view


By registering, I agree to the Terms and Privacy Policies
Already have an account?
Just a few more details

So we can recommend you notes for your school.

Reset Password

Please enter below the email address you registered with and we will send you a link to reset your password.

Add your courses

Get notes from the top students in your class.