Dears,
is it possible for a cysteine to be conformationally disordered? It seems
strange to me. If it were, it would almost certainly be exposed to the
solvent and thus easily oxidized irreversibly. Do you perhaps have any
information on conformationally disordered cysteines?
I thank you,
Oliviero
In a few months, I will retire, because my brain thinks it is still young
but the rest of the body disagrees and thinks the brain is slightly senile.
Of course, I will miss the protein structures very much, so unpredictable
in their insolent beauty.
I have devoted several years of my life to the
operly
> the young
> > generation.
> >
> > I understand your frustation and may be it deserves a letter in an Acta
> > Journal, but please, please, refrain of citing the "ignorants" in this
> bb.
> >
> > Wishing you a happy retirement and nice and
You might try Stride (http://webclu.bio.wzw.tum.de/stride) or 2Struc (
http://2struc.cryst.bbk.ac.uk; which is not available now but was available
some time ago).
Best,
Oliviero
Il giorno mer 13 nov 2024 alle ore 16:31 Robbie Joosten <
robbie_joos...@hotmail.com> ha scritto:
> It is, but it is
l
>be that the motions are correlated across the interface.
>
>
> Pietro
>
> Sent from Outlook for iOS <https://aka.ms/o0ukef>
> ------
> *From:* CCP4 bulletin board on behalf of Italo
> Carugo Oliviero
> *Sent:* Wednesday, October 30, 2024
in question, decompose them into descriptors of elemental
> motions, and assess whether these motions make physical sense in the
> context of the given TLS partitioning. These methods are all detailed in
> the works above, and the tools to do this are available to you!
>
> All t
Dear Tommi,
you could write a program (perhaps with ChatGPT) that (i) stores water
molecules, (ii) stores protein atoms, and (iii) searches, among the water
molecules, for those that are close to two protein atoms that belong to
different chains.
Oliviero
Il giorno mer 6 nov 2024 alle ore 16:43 Ka
A brief reflection on IDPs
Increasingly, people with a computer science background are analyzing the
data deposited in the Protein Data Bank. In the case of conformation
disorder analyses, they consider residues that are explicitly stated to be
disordered (the old REMAR 465 records). This is not
cupancy
> but would also accrue a lower B factor, but I think it is more appropriate
> to model a single favourable conformer that fits the density.
>
>
>
>
>
> This is certainly the first X-ray structure that I ever worked on that was
> quite like this, so id like to hear pe
Just wanted to thank you for your remarkable contributions to this
discussion.
These are a couple of articles that dive into the issue of unusually large
B-factors: BMC Bioinformatics 2018 19 61 (
https://doi.org/10.1186/s12859-018-2083-8) & Zeit. Krist. 2018 234 73-77 (
https://doi.org/10.1515/zk
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