FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1966851556> ?p ?o ?g. }

• W1966851556 endingPage "365" @default.
• W1966851556 startingPage "351" @default.
• W1966851556 abstract "The Zimm-Bragg parameters s and sigma are calculated for the helix-coil transition of poly-L-alanine. The theoretical approach involves evaluating gas phase conformational energies for both coil and helical states using the CHARMM potential function and accounting for solvation effects with various continuum solvation models. Conformational free energies are then incorporated into a formalism developed by Go et al. for the calculation of s and sigma. Calculated values for both s and sigma as well as the enthalpy change associated with helix formation are in good agreement with experimental data when the Finite Difference Poisson-Boltzmann (FDPB) method is used to treat solvent effects. The driving force for the helix-coil transition is analyzed in terms of individual free energy components. Hydrogen bond formation is found to contribute little to helix stability because the internal hydrogen bonding energy is largely canceled by the large free energy cost associated with removing polar groups from water. The entropic cost associated with fixing backbone dihedral angles in the helical conformation is found to be approximately 7 e.u./residue (about 2 kcal/mol at room temperature). The major driving force favoring helix formation can be associated with interactions including enhanced van der Waals interactions in the close-packed helix conformation and the hydrophobic effect. These contribute about 2 kcal/mol favoring the helical state. The differences in helical propensities between alanine and glycine are attributed primarily to hydrophobic and packing interactions involving the C beta with a smaller contribution arising from increased conformational freedom for glycine in the coil state. The description of helix formation presented here is consistent with previous conclusions regarding tertiary structure formation which suggest that hydrophobic and close-packed interactions provide stability while hydrogen bond formation constitutes a structural constraint imposed by the high free energy cost associated with burying unsatisfied hydrogen bonding groups. alpha-Helix formation may thus be viewed as a form of hydrophobic collapse constrained by the requirement that polar groups be either exposed to solvent or form hydrogen bonds. More generally it appears from this study that for a folding model to be a realistic, it must properly account for the chemical nature of the polypeptide chain, particularly the solvation energetics of amide groups." @default.
• W1966851556 created "2016-06-24" @default.
• W1966851556 creator A5014393887 @default.
• W1966851556 creator A5036654109 @default.
• W1966851556 date "1995-09-01" @default.
• W1966851556 modified "2023-10-10" @default.
• W1966851556 title "Free Energy Determinants of Secondary Structure Formation: I. α-Helices" @default.
• W1966851556 doi "https://doi.org/10.1006/jmbi.1995.0502" @default.
• W1966851556 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7563056" @default.
• W1966851556 hasPublicationYear "1995" @default.
• W1966851556 type Work @default.
• W1966851556 sameAs 1966851556 @default.
• W1966851556 citedByCount "212" @default.
• W1966851556 countsByYear W19668515562012 @default.
• W1966851556 countsByYear W19668515562013 @default.
• W1966851556 countsByYear W19668515562014 @default.
• W1966851556 countsByYear W19668515562015 @default.
• W1966851556 countsByYear W19668515562016 @default.
• W1966851556 countsByYear W19668515562017 @default.
• W1966851556 countsByYear W19668515562018 @default.
• W1966851556 countsByYear W19668515562019 @default.
• W1966851556 countsByYear W19668515562020 @default.
• W1966851556 countsByYear W19668515562021 @default.
• W1966851556 countsByYear W19668515562022 @default.
• W1966851556 countsByYear W19668515562023 @default.
• W1966851556 crossrefType "journal-article" @default.
• W1966851556 hasAuthorship W1966851556A5014393887 @default.
• W1966851556 hasAuthorship W1966851556A5036654109 @default.
• W1966851556 hasBestOaLocation W19668515561 @default.
• W1966851556 hasConcept C112887158 @default.
• W1966851556 hasConcept C121332964 @default.
• W1966851556 hasConcept C126061179 @default.
• W1966851556 hasConcept C148093993 @default.
• W1966851556 hasConcept C159467904 @default.
• W1966851556 hasConcept C178790620 @default.
• W1966851556 hasConcept C185592680 @default.
• W1966851556 hasConcept C18903297 @default.
• W1966851556 hasConcept C2778530040 @default.
• W1966851556 hasConcept C2779965526 @default.
• W1966851556 hasConcept C2780471494 @default.
• W1966851556 hasConcept C3288061 @default.
• W1966851556 hasConcept C32909587 @default.
• W1966851556 hasConcept C64147673 @default.
• W1966851556 hasConcept C8010536 @default.
• W1966851556 hasConcept C86803240 @default.
• W1966851556 hasConcept C89025888 @default.
• W1966851556 hasConcept C90260826 @default.
• W1966851556 hasConcept C97355855 @default.
• W1966851556 hasConceptScore W1966851556C112887158 @default.
• W1966851556 hasConceptScore W1966851556C121332964 @default.
• W1966851556 hasConceptScore W1966851556C126061179 @default.
• W1966851556 hasConceptScore W1966851556C148093993 @default.
• W1966851556 hasConceptScore W1966851556C159467904 @default.
• W1966851556 hasConceptScore W1966851556C178790620 @default.
• W1966851556 hasConceptScore W1966851556C185592680 @default.
• W1966851556 hasConceptScore W1966851556C18903297 @default.
• W1966851556 hasConceptScore W1966851556C2778530040 @default.
• W1966851556 hasConceptScore W1966851556C2779965526 @default.
• W1966851556 hasConceptScore W1966851556C2780471494 @default.
• W1966851556 hasConceptScore W1966851556C3288061 @default.
• W1966851556 hasConceptScore W1966851556C32909587 @default.
• W1966851556 hasConceptScore W1966851556C64147673 @default.
• W1966851556 hasConceptScore W1966851556C8010536 @default.
• W1966851556 hasConceptScore W1966851556C86803240 @default.
• W1966851556 hasConceptScore W1966851556C89025888 @default.
• W1966851556 hasConceptScore W1966851556C90260826 @default.
• W1966851556 hasConceptScore W1966851556C97355855 @default.
• W1966851556 hasIssue "3" @default.
• W1966851556 hasLocation W19668515561 @default.
• W1966851556 hasLocation W19668515562 @default.
• W1966851556 hasOpenAccess W1966851556 @default.
• W1966851556 hasPrimaryLocation W19668515561 @default.
• W1966851556 hasRelatedWork W1966793603 @default.
• W1966851556 hasRelatedWork W1974433778 @default.
• W1966851556 hasRelatedWork W2019750909 @default.
• W1966851556 hasRelatedWork W2045242973 @default.
• W1966851556 hasRelatedWork W2048341727 @default.
• W1966851556 hasRelatedWork W2053689559 @default.
• W1966851556 hasRelatedWork W2089507369 @default.
• W1966851556 hasRelatedWork W2105465678 @default.
• W1966851556 hasRelatedWork W2498829061 @default.
• W1966851556 hasRelatedWork W4323037679 @default.
• W1966851556 hasVolume "252" @default.
• W1966851556 isParatext "false" @default.
• W1966851556 isRetracted "false" @default.
• W1966851556 magId "1966851556" @default.
• W1966851556 workType "article" @default.