English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Open

The hydration free energy of a macromolecule is the central property ofinterest for understanding its distribution over conformations and its state ofaggregation. Calculating the hydration free energy of a macromolecule inall-atom simulations has long remained a challenge, necessitating the use ofmodels wherein the effect of the solvent is captured without explicit accountof solvent degrees of freedom. This situation has changed with developments inthe molecular quasi-chemical theory (QCT), an approach that enables calculationof the hydration free energy of macromolecules within all-atom simulations atthe same resolution as is possible for small molecule solutes. The theory alsoprovides a rigorous and physically transparent framework to conceptualize andmodel interactions in molecular solutions, and thus provides a convenientframework to investigate the assumptions in implicit-solvent models. In thisstudy, we compare the results using molecular QCT versus predictions from EEF1,ABSINTH, and GB/SA implicit-solvent models for poly-glycine and poly-alaninesolutes covering a range of chain lengths and conformations. Among the threemodels, GB/SA does best in capturing the broad trends in hydration free energy.We trace the deficiencies of the group-additive EEF1 and ABSINTH models totheir under-appreciation of the cooperativity of hydration between solutegroups; seen in this light, the better performance of GB/SA can be attributedto its treatment of the collective properties of hydration, albeit within acontinuum dielectric framework. We highlight the importance of validating theindividual physical components that enter implicit solvent models for proteinsolution thermodynamics.

Hydration free energies of polypeptides from popular implicit solvent  models versus all-atom simulation results based on molecular quasichemical  theory