My bet is on the journals bending over.. given that the NIH is also going to release new guidelines soon.. it sure is an interesting juncture..!

Sad. Maybe a wall of shame with images of equipment might serve as a useful reminder to future trainees about what not to do..?

Working for me in India right now.. that's all i know. 🤷

How strange.. it is accessible to me in India at the moment.

Haha, yes, i can imagine. Although what has worked for me in the past is just sanding down the contacts, tightening any loose contacts, shielding some wires, and improving the grounding pattern. Best of luck 👍🏻

No..! but, why..?

Not always. Although i agree with your point because the number of publications has increased, but look at this example.

Thanks to the mentorship of Profs P. Balaram, M.K. Mathew and Shachi Gosavi (still not here)

This marks publication of some of my PhD thesis work. More to follow!

Preprint:
www.biorxiv.org/content/10.1...

There are more goodies in the paper. A speculative mechanism of the spike TM helix conformation from prefusion to postfusion state. Utility of simulating self-association of multiple conformers of a single TM helix. Peptides to block this conserved interaction. etc.

We also looked at cholesterol interaction of the TM helix and again, oddly enough cholesterol does not prefer the cholesterol interaction surface on the spike TM helix. Instead, it decreases the propensity of TM helices to self-associate

While I could end here, we find that the spike TM helix can form two kinds of dimers differing in their super-helical handedness (left handed and right handed) stabilized by two different interfaces

Although the symmetric trimers resemble the symmetry of the ectomembrane spike, the asymmetric trimer could stabilize the fusion intermediates, which are also asymmetric

We coarse grained three atomistically derived conformations that differed in their membrane exposure and tilt w.r.t. the membrane normal, and started 100s of martini relaxations to find 2 kinds of trimers: symmetric and asymmetric

These movements of the spike TM helix in the membrane environment cause local thinning of the membrane, which we feel could be important for viral fusion

So, we started by atomistically determining the membrane exposed region of the spike protein. Turns out the spike TM is highly dynamic: bobbing, tilting, gaining and losing helicity at the membrane ends

We focused on the spike transmembrane domain (TMD), which like many other membrane proteins is overlooked and understudied. Turns out, the single TM helix is >30 residues long, coming at the tail of TM length distribution of naturally occurring proteins (22-25 residues)

Text is forgettable, but the mental image created by the figure alongside the term "alternating access" is so much more memorable.

Thanks for including the doi to the original paper and to others for the examples