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 < 000030c2162795b2-dmarc-requ...@jiscmail.ac.uk> 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 > > ------------------------------ > > To unsubscribe from the CCP4BB list, click the following link: > https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 > ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
