FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1996127247> ?p ?o ?g. }

• W1996127247 endingPage "816" @default.
• W1996127247 startingPage "807" @default.
• W1996127247 abstract "Determining the structure of the transition state is critical for elucidating the mechanism behind how proteins fold and unfold. Due to its high free energy, however, the transition state generally cannot be trapped and studied directly using traditional structural biology methods. Thus, characterizing the structure of the transition state that occurs as proteins fold and unfold remains a major challenge. Here, we report a novel (to our knowledge) method that uses engineered bi-histidine (bi-His) metal-binding sites to directly map the structure of the mechanical unfolding transition state of proteins. This method is adapted from the traditional ψ-value analysis, which uses engineered bi-His metal chelation sites to probe chemical (un)folding transition-state structure. The φ(M2+)(U)-value is defined as ΔΔG(‡-N)/ΔΔG(U-N), which is the energetic effects of metal chelation by the bi-His site on the unfolding energy barrier (ΔG(‡-N)) relative to its thermodynamic stability (ΔG(U-N)) and can be used to obtain information about the transition state in the mutational site. As a proof of principle, we used the small protein GB1 as a model system and set out to map its mechanical unfolding transition-state structure. Using single-molecule atomic force microscopy and spectrofluorimetry, we directly quantified the effect of divalent metal ion binding on the mechanical unfolding free energy and thermodynamic stability of GB1, which allowed us to quantify φ(M2+)(U)-values for different sites in GB1. Our results enabled us to map the structure of the mechanical unfolding transition state of GB1. Within GB1's mechanical unfolding transition state, the interface between force-bearing β-strands 1 and 4 is largely disrupted, and the first β-hairpin is partially disordered while the second β-hairpin and the α-helix remain structured. Our results demonstrate the unique application of ψ-value analysis in elucidating the structure of the transition state that occurs during the mechanical unfolding process, offering a potentially powerful new method for investigating the design of novel elastomeric proteins." @default.
• W1996127247 created "2016-06-24" @default.
• W1996127247 creator A5001594847 @default.
• W1996127247 creator A5028786072 @default.
• W1996127247 creator A5030144808 @default.
• W1996127247 creator A5042726750 @default.
• W1996127247 date "2012-08-01" @default.
• W1996127247 modified "2023-10-13" @default.
• W1996127247 title "Engineered Bi-Histidine Metal Chelation Sites Map the Structure of the Mechanical Unfolding Transition State of an Elastomeric Protein Domain GB1" @default.
• W1996127247 cites W1505900198 @default.
• W1996127247 cites W1534116117 @default.
• W1996127247 cites W1538731614 @default.
• W1996127247 cites W1570122994 @default.
• W1996127247 cites W1579363245 @default.
• W1996127247 cites W1978033776 @default.
• W1996127247 cites W1982383374 @default.
• W1996127247 cites W1983824687 @default.
• W1996127247 cites W1991653374 @default.
• W1996127247 cites W1996631886 @default.
• W1996127247 cites W2008440654 @default.
• W1996127247 cites W2016388018 @default.
• W1996127247 cites W2020716464 @default.
• W1996127247 cites W2029871341 @default.
• W1996127247 cites W2037155044 @default.
• W1996127247 cites W2037670051 @default.
• W1996127247 cites W2037720334 @default.
• W1996127247 cites W2044754051 @default.
• W1996127247 cites W2047510784 @default.
• W1996127247 cites W2049028119 @default.
• W1996127247 cites W2049535263 @default.
• W1996127247 cites W2050410320 @default.
• W1996127247 cites W2052776438 @default.
• W1996127247 cites W2053961215 @default.
• W1996127247 cites W2060841475 @default.
• W1996127247 cites W2068049270 @default.
• W1996127247 cites W2069384750 @default.
• W1996127247 cites W2069629599 @default.
• W1996127247 cites W2078043123 @default.
• W1996127247 cites W2082120576 @default.
• W1996127247 cites W2085458671 @default.
• W1996127247 cites W2086579456 @default.
• W1996127247 cites W2090777935 @default.
• W1996127247 cites W2091114929 @default.
• W1996127247 cites W2117481749 @default.
• W1996127247 cites W2131439250 @default.
• W1996127247 cites W2143848552 @default.
• W1996127247 cites W2147749191 @default.
• W1996127247 cites W2158476854 @default.
• W1996127247 cites W2169529439 @default.
• W1996127247 cites W2329630164 @default.
• W1996127247 doi "https://doi.org/10.1016/j.bpj.2012.07.019" @default.
• W1996127247 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3443793" @default.
• W1996127247 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22947942" @default.
• W1996127247 hasPublicationYear "2012" @default.
• W1996127247 type Work @default.
• W1996127247 sameAs 1996127247 @default.
• W1996127247 citedByCount "16" @default.
• W1996127247 countsByYear W19961272472012 @default.
• W1996127247 countsByYear W19961272472013 @default.
• W1996127247 countsByYear W19961272472014 @default.
• W1996127247 countsByYear W19961272472015 @default.
• W1996127247 countsByYear W19961272472016 @default.
• W1996127247 countsByYear W19961272472018 @default.
• W1996127247 countsByYear W19961272472020 @default.
• W1996127247 countsByYear W19961272472021 @default.
• W1996127247 countsByYear W19961272472023 @default.
• W1996127247 crossrefType "journal-article" @default.
• W1996127247 hasAuthorship W1996127247A5001594847 @default.
• W1996127247 hasAuthorship W1996127247A5028786072 @default.
• W1996127247 hasAuthorship W1996127247A5030144808 @default.
• W1996127247 hasAuthorship W1996127247A5042726750 @default.
• W1996127247 hasBestOaLocation W19961272471 @default.
• W1996127247 hasConcept C106773901 @default.
• W1996127247 hasConcept C119599485 @default.
• W1996127247 hasConcept C119621388 @default.
• W1996127247 hasConcept C127413603 @default.
• W1996127247 hasConcept C159467904 @default.
• W1996127247 hasConcept C161790260 @default.
• W1996127247 hasConcept C178790620 @default.
• W1996127247 hasConcept C185592680 @default.
• W1996127247 hasConcept C186399102 @default.
• W1996127247 hasConcept C19472624 @default.
• W1996127247 hasConcept C204328495 @default.
• W1996127247 hasConcept C2776545253 @default.
• W1996127247 hasConcept C2778460671 @default.
• W1996127247 hasConcept C47701112 @default.
• W1996127247 hasConcept C515207424 @default.
• W1996127247 hasConcept C55493867 @default.
• W1996127247 hasConcept C8010536 @default.
• W1996127247 hasConceptScore W1996127247C106773901 @default.
• W1996127247 hasConceptScore W1996127247C119599485 @default.
• W1996127247 hasConceptScore W1996127247C119621388 @default.
• W1996127247 hasConceptScore W1996127247C127413603 @default.
• W1996127247 hasConceptScore W1996127247C159467904 @default.
• W1996127247 hasConceptScore W1996127247C161790260 @default.
• W1996127247 hasConceptScore W1996127247C178790620 @default.
• W1996127247 hasConceptScore W1996127247C185592680 @default.
• W1996127247 hasConceptScore W1996127247C186399102 @default.

• next