Matches in SemOpenAlex for { <https://semopenalex.org/work/W2087596395> ?p ?o ?g. }
- W2087596395 endingPage "14369" @default.
- W2087596395 startingPage "14361" @default.
- W2087596395 abstract "Helix-helix interactions within membranes are dominated by van der Waals packing motifs and side chain-side chain hydrogen bond formation, which act in tandem to determine the residues that comprise the interface between two given helices. To explore in a systematic manner the tertiary contacts between transmembrane helices, we have designed and expressed in Escherichia coli highly hydrophobic helix-loop-helix constructs of prototypic sequence K(1)KKKKKKFAIAIAIIAWAX(19)AIIAIAIAIKSPGSKIAIAIAIIAZ(44)AWAIIAIAIAFKKKKKKK(62), where small (Ala) and large (Ile) residues were used to maximize the tertiary contact area. Evidence that the two transmembrane (TM) segments in the AI construct contain an interface conducive for folding into a hairpin structure was obtained from the results that (i) the single TM AI(pep) peptide derived from the AI hairpin forms SDS-resistant dimers on PAGE gels and (ii) the corresponding sequence forms a strong dimer when examined in vivo in TOXCAT assays. Site-directed mutagenesis of AI hairpins was carried out to incorporate each of the 20 commonly occurring amino acids at X positions. Analysis on Western blots using an oligomerization assay in 12% NuPage-sodium dodecyl sulfate (SDS) indicated that mutants with X = E, D, Q, R, N, H, and K largely formed SDS-resistant dimers-which likely correspond to H-bonded four-helix bundles-while all the others (e.g., X = F, W, L, I, M, V, C, Y, A, T, S, G, and P) remained monomeric. Systematic studies of X/Z double mutants indicated that formation of hairpin dimers is the result of the disruption of stabilizing interactions between the antiparallel helices within the AI construct. The overall results suggest that, in situations where hydrophobic van der Waals packing energy between helices is sufficient to prevent significant rotation about the major axes of interacting helices, intrahairpin side chain-side chain H-bond formation will occur mainly when pairs of polar residues are interfacially located and proximal. Knowledge of the relative contributions of these forces should be of value, for example, in clarifying the context--and the structural consequences--of disease-related mutations." @default.
- W2087596395 created "2016-06-24" @default.
- W2087596395 creator A5003899670 @default.
- W2087596395 creator A5038272193 @default.
- W2087596395 creator A5041060172 @default.
- W2087596395 date "2004-10-21" @default.
- W2087596395 modified "2023-10-14" @default.
- W2087596395 title "Hydrophobic Helical Hairpins: Design and Packing Interactions in Membrane Environments" @default.
- W2087596395 cites W2020933513 @default.
- W2087596395 cites W2033323125 @default.
- W2087596395 cites W2039587858 @default.
- W2087596395 cites W2040030304 @default.
- W2087596395 cites W2046524985 @default.
- W2087596395 cites W2049097938 @default.
- W2087596395 cites W2059451993 @default.
- W2087596395 cites W2080301705 @default.
- W2087596395 cites W2083768931 @default.
- W2087596395 cites W2090564123 @default.
- W2087596395 cites W2094186244 @default.
- W2087596395 cites W2097761188 @default.
- W2087596395 cites W2104597743 @default.
- W2087596395 cites W2124961727 @default.
- W2087596395 cites W2168048273 @default.
- W2087596395 doi "https://doi.org/10.1021/bi0492760" @default.
- W2087596395 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15533040" @default.
- W2087596395 hasPublicationYear "2004" @default.
- W2087596395 type Work @default.
- W2087596395 sameAs 2087596395 @default.
- W2087596395 citedByCount "37" @default.
- W2087596395 countsByYear W20875963952012 @default.
- W2087596395 countsByYear W20875963952013 @default.
- W2087596395 countsByYear W20875963952015 @default.
- W2087596395 countsByYear W20875963952016 @default.
- W2087596395 countsByYear W20875963952019 @default.
- W2087596395 countsByYear W20875963952020 @default.
- W2087596395 countsByYear W20875963952022 @default.
- W2087596395 crossrefType "journal-article" @default.
- W2087596395 hasAuthorship W2087596395A5003899670 @default.
- W2087596395 hasAuthorship W2087596395A5038272193 @default.
- W2087596395 hasAuthorship W2087596395A5041060172 @default.
- W2087596395 hasConcept C104317684 @default.
- W2087596395 hasConcept C112887158 @default.
- W2087596395 hasConcept C118892022 @default.
- W2087596395 hasConcept C119599485 @default.
- W2087596395 hasConcept C126061179 @default.
- W2087596395 hasConcept C127413603 @default.
- W2087596395 hasConcept C133571119 @default.
- W2087596395 hasConcept C143065580 @default.
- W2087596395 hasConcept C16318435 @default.
- W2087596395 hasConcept C170493617 @default.
- W2087596395 hasConcept C178790620 @default.
- W2087596395 hasConcept C185592680 @default.
- W2087596395 hasConcept C18903297 @default.
- W2087596395 hasConcept C204921945 @default.
- W2087596395 hasConcept C24530287 @default.
- W2087596395 hasConcept C2776545253 @default.
- W2087596395 hasConcept C2778530040 @default.
- W2087596395 hasConcept C2779546866 @default.
- W2087596395 hasConcept C2779965526 @default.
- W2087596395 hasConcept C32909587 @default.
- W2087596395 hasConcept C41625074 @default.
- W2087596395 hasConcept C47701112 @default.
- W2087596395 hasConcept C521977710 @default.
- W2087596395 hasConcept C55493867 @default.
- W2087596395 hasConcept C71240020 @default.
- W2087596395 hasConcept C8010536 @default.
- W2087596395 hasConcept C86803240 @default.
- W2087596395 hasConceptScore W2087596395C104317684 @default.
- W2087596395 hasConceptScore W2087596395C112887158 @default.
- W2087596395 hasConceptScore W2087596395C118892022 @default.
- W2087596395 hasConceptScore W2087596395C119599485 @default.
- W2087596395 hasConceptScore W2087596395C126061179 @default.
- W2087596395 hasConceptScore W2087596395C127413603 @default.
- W2087596395 hasConceptScore W2087596395C133571119 @default.
- W2087596395 hasConceptScore W2087596395C143065580 @default.
- W2087596395 hasConceptScore W2087596395C16318435 @default.
- W2087596395 hasConceptScore W2087596395C170493617 @default.
- W2087596395 hasConceptScore W2087596395C178790620 @default.
- W2087596395 hasConceptScore W2087596395C185592680 @default.
- W2087596395 hasConceptScore W2087596395C18903297 @default.
- W2087596395 hasConceptScore W2087596395C204921945 @default.
- W2087596395 hasConceptScore W2087596395C24530287 @default.
- W2087596395 hasConceptScore W2087596395C2776545253 @default.
- W2087596395 hasConceptScore W2087596395C2778530040 @default.
- W2087596395 hasConceptScore W2087596395C2779546866 @default.
- W2087596395 hasConceptScore W2087596395C2779965526 @default.
- W2087596395 hasConceptScore W2087596395C32909587 @default.
- W2087596395 hasConceptScore W2087596395C41625074 @default.
- W2087596395 hasConceptScore W2087596395C47701112 @default.
- W2087596395 hasConceptScore W2087596395C521977710 @default.
- W2087596395 hasConceptScore W2087596395C55493867 @default.
- W2087596395 hasConceptScore W2087596395C71240020 @default.
- W2087596395 hasConceptScore W2087596395C8010536 @default.
- W2087596395 hasConceptScore W2087596395C86803240 @default.
- W2087596395 hasIssue "45" @default.
- W2087596395 hasLocation W20875963951 @default.
- W2087596395 hasLocation W20875963952 @default.
- W2087596395 hasOpenAccess W2087596395 @default.