FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2155706673> ?p ?o ?g. }

• W2155706673 endingPage "337" @default.
• W2155706673 startingPage "325" @default.
• W2155706673 abstract "The α-helix remains a focus of research because of its importance to protein folding and structure. Nevertheless, despite numerous empirical, computational, and theoretical studies, the fundamental structural properties governing their formation and stability are still unclear. We have examined the statistical occurrence of polar and apolar residue patterning in helical interiors in a large, non-redundant dataset, and compared these patterns with those found in other structural environments. While the familiar amphipathic distributions for both polar and apolar residues are evident, our analysis also finds significant differences between these distributions. Non-amphipathic signals can also be discerned within both distributions. Most interestingly, among various positional patterning, an analysis of immediate (i,i + 1) helical neighbours found: (i) clear neighbouring preferences, with high (low) occurrences of hydrophobics (hydrophilics) next to Gly, Pro, and short polar residues; (ii) high negative (positive) correlation between residue helical propensities and the degree of neighbouring hydrophobicity (hydrophilicity); and (iii) a preferred ordering among neighbours, implying an inherent helix directionality. Because (i,i + 1) helical pairs have limited side chain – side chain interactions, thermodynamic considerations cannot readily explain these observations, nor can evolutionary pressures that enhance tertiary interactions via amphipathicity, as this particular spacing does not segregate residues onto either the same or opposing helical faces. We suggest that the mechanism of helix formation may be partly responsible for these observations. In particular, the high negative correlation between residue helical propensities and neighbouring hydrophobicity suggests that hydrophobicity may play a more important role in helix formation than currently recognized." @default.
• W2155706673 created "2016-06-24" @default.
• W2155706673 creator A5050847765 @default.
• W2155706673 creator A5063683282 @default.
• W2155706673 date "2010-04-01" @default.
• W2155706673 modified "2023-09-27" @default.
• W2155706673 title "Residue patterning in helix interiorsThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process." @default.
• W2155706673 cites W1758266623 @default.
• W2155706673 cites W1963550288 @default.
• W2155706673 cites W1968712781 @default.
• W2155706673 cites W1972698196 @default.
• W2155706673 cites W1999004357 @default.
• W2155706673 cites W1999009652 @default.
• W2155706673 cites W2003822472 @default.
• W2155706673 cites W2008357770 @default.
• W2155706673 cites W2008708467 @default.
• W2155706673 cites W2014059004 @default.
• W2155706673 cites W2014095962 @default.
• W2155706673 cites W2021106586 @default.
• W2155706673 cites W2022008275 @default.
• W2155706673 cites W2046610667 @default.
• W2155706673 cites W2055680113 @default.
• W2155706673 cites W2056770911 @default.
• W2155706673 cites W2072495252 @default.
• W2155706673 cites W2075925635 @default.
• W2155706673 cites W2077895595 @default.
• W2155706673 cites W2078551614 @default.
• W2155706673 cites W2079492386 @default.
• W2155706673 cites W2081359387 @default.
• W2155706673 cites W2082329958 @default.
• W2155706673 cites W2092880728 @default.
• W2155706673 cites W2101152106 @default.
• W2155706673 cites W2103228844 @default.
• W2155706673 cites W2114277014 @default.
• W2155706673 cites W2116449290 @default.
• W2155706673 cites W2126912623 @default.
• W2155706673 cites W2130663065 @default.
• W2155706673 cites W2137189075 @default.
• W2155706673 cites W2138169197 @default.
• W2155706673 cites W2139739021 @default.
• W2155706673 cites W2140992384 @default.
• W2155706673 cites W2141810500 @default.
• W2155706673 cites W2146210326 @default.
• W2155706673 cites W2146242951 @default.
• W2155706673 cites W2150654191 @default.
• W2155706673 cites W2159044609 @default.
• W2155706673 cites W2159609845 @default.
• W2155706673 cites W3047703793 @default.
• W2155706673 cites W4244926109 @default.
• W2155706673 doi "https://doi.org/10.1139/o09-156" @default.
• W2155706673 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20453933" @default.
• W2155706673 hasPublicationYear "2010" @default.
• W2155706673 type Work @default.
• W2155706673 sameAs 2155706673 @default.
• W2155706673 citedByCount "2" @default.
• W2155706673 countsByYear W21557066732016 @default.
• W2155706673 crossrefType "journal-article" @default.
• W2155706673 hasAuthorship W2155706673A5050847765 @default.
• W2155706673 hasAuthorship W2155706673A5063683282 @default.
• W2155706673 hasConcept C119599485 @default.
• W2155706673 hasConcept C121332964 @default.
• W2155706673 hasConcept C12554922 @default.
• W2155706673 hasConcept C127413603 @default.
• W2155706673 hasConcept C1276947 @default.
• W2155706673 hasConcept C147597530 @default.
• W2155706673 hasConcept C15920480 @default.
• W2155706673 hasConcept C178790620 @default.
• W2155706673 hasConcept C185592680 @default.
• W2155706673 hasConcept C18903297 @default.
• W2155706673 hasConcept C204328495 @default.
• W2155706673 hasConcept C2776545253 @default.
• W2155706673 hasConcept C2778530040 @default.
• W2155706673 hasConcept C2779965526 @default.
• W2155706673 hasConcept C2781338088 @default.
• W2155706673 hasConcept C29705727 @default.
• W2155706673 hasConcept C47701112 @default.
• W2155706673 hasConcept C521977710 @default.
• W2155706673 hasConcept C55493867 @default.
• W2155706673 hasConcept C59593255 @default.
• W2155706673 hasConcept C67407626 @default.
• W2155706673 hasConcept C71240020 @default.
• W2155706673 hasConcept C8010536 @default.
• W2155706673 hasConcept C86803240 @default.
• W2155706673 hasConceptScore W2155706673C119599485 @default.
• W2155706673 hasConceptScore W2155706673C121332964 @default.
• W2155706673 hasConceptScore W2155706673C12554922 @default.
• W2155706673 hasConceptScore W2155706673C127413603 @default.
• W2155706673 hasConceptScore W2155706673C1276947 @default.
• W2155706673 hasConceptScore W2155706673C147597530 @default.
• W2155706673 hasConceptScore W2155706673C15920480 @default.
• W2155706673 hasConceptScore W2155706673C178790620 @default.
• W2155706673 hasConceptScore W2155706673C185592680 @default.
• W2155706673 hasConceptScore W2155706673C18903297 @default.
• W2155706673 hasConceptScore W2155706673C204328495 @default.
• W2155706673 hasConceptScore W2155706673C2776545253 @default.
• W2155706673 hasConceptScore W2155706673C2778530040 @default.
• W2155706673 hasConceptScore W2155706673C2779965526 @default.
• W2155706673 hasConceptScore W2155706673C2781338088 @default.

• next