Dear Sahil,I quickly read part of the paper that you sent. It is very
interesting. Thank you for sharing. Looking forward to read it in details.Best
regards,Samer
On Friday, August 7, 2020, 02:19:20 PM GMT+1, Sahil Batra
<[email protected]> wrote:
Hi Samer,
I came across this interesting article recently, that discusses the
significance of unusually high content of Met in the polymerization inducing
domain of spider silk protein
(https://www.nature.com/articles/s41467-019-12365-5).
Methionines provide a 'mobilization' to the hydrophobic core (something which
no other aliphatic amino acid can), which allows this domain to access
conformational space, and apparently is important for dimerization. It does not
directly answer your question, but seems an interesting read.
Best regards,
Sahil Batra
On Fri, Aug 7, 2020 at 5:44 PM samer halabi
<[email protected]> wrote:
Dear All,I am working on structures where Methionine is important in binding of
peptides to the MHC protein complex.Would anyone kindly like to share their
knowledge about anything they find it important about this particular amino
acid structurally? Sharing a paper or just few comments will be greatly
appreciated.
I know my question may sound very general (and kind of superficial) but there
is definitely a reason, that I don't know and might be already known, why
certain peptides (like CLIP) are rich in Methionine, and that lowers their
affinity of binding.Thank you and sorry to disturb you all.Best regards,Samer
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