Question 1 of 10 Question 1. If you were to engineer some non- adhesive cells to express E-cadherin at either high levels or low levels and then mixed the E-cadherin high cells with the E-cadherin low cells, what do you predict will happen?

Question 10 of 10 Question 10: What percent of the human genome encodes protein?

Sort each of the following events into those required and those not required for CaM activation of downstream proteins including AtSR 1. Items (5 items) (Drag and drop into the appropriate area below) Two Ca²+ ions are bound to the helical region of calmodulin. Categories Calmodulin wraps tightly around target proteins to activate them. 18 OF 20 QUESTIONS COMPLETED 1 1 1 1 The central helix of calmodulin changes shape to wrap around the target protein. Required Ca2+ ions are released to cause calmodulin to bind more tightly to target proteins. I 1 I I I 1 1 1 I I Ca2+ binding causes dimerization of the calmodulin protein leading. to AtSR1 binding and activation Not required 4 4 VIEW SOLUTION SUBMIT ANS

Which two coat proteins are involved in the bidirectional (two-way) trafficking of the KDEL receptor?     COP II and clathrin     COP I and COP II     clathrin and dynamin     COP I and clathrin

What's the difference between a symporter versus an antiporter? Give an example of each to explain the physiological phenomenon at work.

i found this past paper however i cannot find the solutions, please can you answer question 1c

Same question but two different sections

What would most likely occur to nuclear-cytoplasmic shuttling if the intrinsic GTPase activity of RAN was slowed down by 50%?   Group of answer choices RAN would not bind exportin and proteins would accumulate in the nucleus All of the answers are likely None of the answers are likely Importin beta would not release from RAN in the cytoplasm and nuclear import would slow down RAN would not bind to importin beta and protein cargo in the nucleus would not release

The S (spike) glycoprotein of coronaviruses can engage receptors by the N-terminal domain, the C-terminal domain, or both. The C-terminal domains of both human SARS coronaviruses bind ACE2 (angiotensin-converting enzyme 2), whereas that of MERS-CoV binds DDP4 (dipeptidyl peptidase 4). In contrast, in mouse hepatitis coronavirus (MHV) the N-terminal domain of S binds CEACAM (cell adhesion molecule 1). You have identified a novel coronavirus with an S protein that displays similarity to MHV at the N terminus and to SARS at the C terminus. What are the molecules most likely to function as receptors and how will you test this?

While studying the secretory pathway, you make the following observation about proteins destined for the ER: Proteins translated in vitro in the absence of microsomes migrate more slowly on an SDS PAGE gel than those translated in the presence of microsomes.  What might account for the observed protein size difference?       A. SRP, present only in microsomes, and binds to and removes the signal sequence from the protein, resulting in a protein is smaller and migrates more quickly on a gel.       B.   Signal peptidase, present only in the microsomes, cleaves the signal sequence from the protein, making the protein smaller and therefore migrate more quickly.     C.   In vitro translated proteins tend to be larger due to a more stable poly A tail      D.   Signal peptidase, present only in the microsomes, adds a signal sequence to the protein, making the protein larger and therefore migrate more slowly.