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Protein phosphorylation

Discussion of all aspects of biological molecules, biochemical processes and laboratory procedures in the field.

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Protein phosphorylation

Postby mrsscientist » Sun Jul 10, 2005 2:43 pm

Can anyone help explain the process of Protein phosphorylation please.
mrsscientist
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Postby Poison » Sun Jul 10, 2005 5:58 pm

I don't know the level of info you need to know about but as a start have a look at this:

http://en.wikipedia.org/wiki/Phosphorylation

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... :P ):

http://www.google.com.tr/search?hl=tr&q ... +Ara&meta=
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How charged with punishment the scroll
I am the Master of my fate
I am the Captain of my soul.
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Postby kk » Mon Aug 03, 2009 9:37 am

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!
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