The optimisation of the helix/helix interaction of a transmembrane dimer is improved by the IMPALA restraint field
Biochimica et Biophysica Acta (BBA) - Biomembranes, ISSN: 0005-2736, Vol: 1509, Issue: 1, Page: 148-154
2000
- 14Citations
- 11Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations14
- Citation Indexes14
- 14
- CrossRef9
- Captures11
- Readers11
- 11
Article Description
A continuous membrane model (IMPALA) was previously developed to predict how hydrophobic spans of proteins insert in membranes (Mol. Mod. 2 (1996) 27). Using that membrane model, we looked for the interactions between several hydrophobic spans. We used the glycophorin A dimer as an archetype of polytopic protein to validate the approach. We find that the native complex do not dislocate when it is submitted to a 10 5 steps optimisation whereas separated spans converge back to a native-like complex in the same conditions. We also observe that IMPALA restraints are not strictly mandatory but do increase the efficiency of the procedure.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S000527360000290X; http://dx.doi.org/10.1016/s0005-2736(00)00290-x; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0034695053&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/11118526; http://linkinghub.elsevier.com/retrieve/pii/S000527360000290X; http://api.elsevier.com/content/article/PII:S000527360000290X?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S000527360000290X?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S000527360000290X; http://dx.doi.org/10.1016/s0005-2736%2800%2900290-x; https://dx.doi.org/10.1016/s0005-2736%2800%2900290-x
Elsevier BV
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