Can anyone help explain the process of Protein phosphorylation please.
I don’t know the level of info you need to know about but as a start have a look at this:
For more, make a google search or click the link below. I’m in my good day I made the search for you. ( I know, It isn’t hard… 😛 ):
http://www.google.com.tr/search?hl=tr&q … +Ara&meta=
My question is regarding mimicing of protein phosphorylation. Changing a serine (Ser) amino acid residue to aspartic acid (Asp) or glutamic acid (Glu) supposedly mimics a phosphorylated serine.
1. How much is it mimicing, can I accept my results based on the presence or Asp/Glu is if my protein was Ser-phosphorylated?
2. Is it simply mimicing because the presence of the -COOH group in Asp/Glu is similar to a phosphate group?
3. Can Asp/Glu mimic threonine (Thr) or tyrosine (Tyr) phosphorylations as well? I guess it could for Thr as well, since Ser and Thr are very similar in shape.
Thanks in advance!