JW: I was under the impression that ff14sb performed best with tip3p
Null 0.0.3 OPC does keep GB3 stabilized but does not fold 15-mer
LS: I’m excited that Null 0.0.3 + OPC passes all tests except the 15-mer
CC: Specific 0.0.3 folds 15-mer with all 4 water models on slide 18. But GB3 helix still destabilized
CC: we had wanted a force field to pass both the 15-mer and GB3 benchmarks before starting the next step. Is that still the case?
MS: most single helices aren’t super stable – is a single alpha helical peptide too stringent a criterion?
CC: I think for this temperature (274 K), it’s roughly 50% helix and comparing the chemical shift not too stringent
MS: previously mentioned using a different library of conformers …? (~34 min)
CC: should we keep probing Null 0.0.3 + OPC
AF: not a lot of man hours, can do a check after a couple microseconds
DLM: if we can get a FF that works well with a 4 point water model vs spending more years on a 3 point one, I’d choose the first. We can hedge our bets here.
Consensus: keep running other folded proteins while CC continues other pathways of investigation
JW: do you have feelings about showing an in-progress protein FF at the annual meeting? We’re doing a tech demo and could feature it with warnings
CC: it depends. Not enthusiastic if it causes too much excitement
CC: a positive outcome is that it could demonstrate that we are closer to our goal from last year
DLM: we should put this in the annual report
JW: ok, won’t present live progress on protein FF
