Test #1 Review Flashcards
Define Chaperones
Proteins whose job is to help other protein fold or keep them unfolded
What type of molecule is a Chaperone ?
A protein
Define Disulfide Bonds
A critical type of folding
Explain tertiary Structure in Protein Folding
Binding to an amino acid cystine.
How does cystine obtain its shape ?
Cystine will bond to one another to give shape
Why are Cysteins important ?
Help shape the proteins
Define Cleavage
Sequences that are removed during proccesing
What is an example of cleavage?
We make pre-insulin. Pre-insulin will get stuck in the translocon. We cleave the “pre” part so that is can fit through and go to the ER.
What do sugars act as ?
Receptors
What do lipids allow a protein to do ?
Allows them to bind to a protein
What is myristoylation and how does it work ?
Adding a lipid to a protein
What are the three parts of processing ?
Folding, Cleavage and addition of sugar or lipid groups
What is allosteric inhibition ?
Binds to any active or non active site
What is competitive inhibtion ?
Binds only to active sites
What is an active site ?
A place a protein can bind
Define phosphorylation
Fast way to turn proteins on and off
Dephosphorylation
Removal of a phosphate
How do phosphates regulate enzyme activity ?
They’re added to the OH sides of serine, threonine and tyrosine
What are the different types of phosphorylation ?
Serine, Therorine and Tyrosine
What enzymes are responsible for adding and removing phosphates ?
Phosphatases
Define protein-protein interactions
proteins that form multi-protein complexes
How do interactions between proteins regulate their activities
A repressor prevents kinases targeting other proteins
Define Ubiquitination
A protein that marks others for degradation by binding to them
What are the steps in Ubiquitination ?
Ubiquitin > Target Protein > Polyubiquitination > Proteasome > Polypeptides