FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2015142802> ?p ?o ?g. }

• W2015142802 endingPage "577" @default.
• W2015142802 startingPage "569" @default.
• W2015142802 abstract "There is currently a great deal of interest in proteins that fold in a single highly cooperative step. Particular attention has been focused on elucidating the factors that govern folding rates of simple proteins. Recently, the topology of the native state has been proposed to be the most important determinant of their folding rates. Here we report a comparative study of the folding of three topologically equivalent proteins that adapt a particularly simple alpha/beta fold. The folding kinetics of the N-terminal domain of RNase HI and the N-terminal domain of the ribosomal protein L9 from Escherichia coli (eNTL9) were compared to the previously characterized N-terminal domain of L9 from Bacillus stearothermophilus (bNTL9). This 6.2 kDa protein, which is one of simplest examples of the ABCalphaD motif, folds via a two-state mechanism on the millisecond to submillisecond time scale. The RNase HI domain and bNTL9 have very similar tertiary structures but there is little similarity in primary sequence. bNTL9 and eNTL9 share the same biological function and a similar primary sequence but differ significantly in stability. Fluorescence-detected stopped-flow experiments showed that the three proteins fold in a two-state fashion. The folding rates in the absence of denaturant were found to be very different, ranging form 21 s(-1) to 790 s(-1) at 10 degrees C. The diverse folding rates appear to reflect large differences in the stability of the proteins. When compared at an isostability point, the folding rates converged to a similar value and there is a strong linear correlation between the log of the folding rate and stability for this set of proteins. These observations are consistent with the idea that stability can play an important role in dictating relative folding rates among topologically equivalent proteins." @default.
• W2015142802 created "2016-06-24" @default.
• W2015142802 creator A5024946575 @default.
• W2015142802 creator A5044356027 @default.
• W2015142802 creator A5049680513 @default.
• W2015142802 date "2001-09-01" @default.
• W2015142802 modified "2023-10-13" @default.
• W2015142802 title "On the Relationship Between Protein Stability and Folding Kinetics: A Comparative Study of the N-terminal Domains of RNase HI, E. coli and Bacillus stearothermophilus L9" @default.
• W2015142802 cites W1526967281 @default.
• W2015142802 cites W1967580376 @default.
• W2015142802 cites W1968470145 @default.
• W2015142802 cites W1973706355 @default.
• W2015142802 cites W1978167946 @default.
• W2015142802 cites W1989297730 @default.
• W2015142802 cites W2022915717 @default.
• W2015142802 cites W2025026970 @default.
• W2015142802 cites W2028231353 @default.
• W2015142802 cites W2031738892 @default.
• W2015142802 cites W2039215531 @default.
• W2015142802 cites W2042236258 @default.
• W2015142802 cites W2044703761 @default.
• W2015142802 cites W2045777307 @default.
• W2015142802 cites W2049864329 @default.
• W2015142802 cites W2056587991 @default.
• W2015142802 cites W2059400471 @default.
• W2015142802 cites W2069568562 @default.
• W2015142802 cites W2071505280 @default.
• W2015142802 cites W2071585569 @default.
• W2015142802 cites W2075505388 @default.
• W2015142802 cites W2082176608 @default.
• W2015142802 cites W2082672971 @default.
• W2015142802 cites W2088780328 @default.
• W2015142802 cites W2088981849 @default.
• W2015142802 cites W2089597488 @default.
• W2015142802 cites W2104704906 @default.
• W2015142802 cites W2115824900 @default.
• W2015142802 cites W2117747873 @default.
• W2015142802 cites W2130949317 @default.
• W2015142802 cites W2165028383 @default.
• W2015142802 cites W2166880005 @default.
• W2015142802 cites W4321429423 @default.
• W2015142802 doi "https://doi.org/10.1006/jmbi.2001.4968" @default.
• W2015142802 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11563917" @default.
• W2015142802 hasPublicationYear "2001" @default.
• W2015142802 type Work @default.
• W2015142802 sameAs 2015142802 @default.
• W2015142802 citedByCount "12" @default.
• W2015142802 countsByYear W20151428022023 @default.
• W2015142802 crossrefType "journal-article" @default.
• W2015142802 hasAuthorship W2015142802A5024946575 @default.
• W2015142802 hasAuthorship W2015142802A5044356027 @default.
• W2015142802 hasAuthorship W2015142802A5049680513 @default.
• W2015142802 hasConcept C104317684 @default.
• W2015142802 hasConcept C10879258 @default.
• W2015142802 hasConcept C119599485 @default.
• W2015142802 hasConcept C121332964 @default.
• W2015142802 hasConcept C12554922 @default.
• W2015142802 hasConcept C127413603 @default.
• W2015142802 hasConcept C148898269 @default.
• W2015142802 hasConcept C162203774 @default.
• W2015142802 hasConcept C185592680 @default.
• W2015142802 hasConcept C19472624 @default.
• W2015142802 hasConcept C204328495 @default.
• W2015142802 hasConcept C206276672 @default.
• W2015142802 hasConcept C2776545253 @default.
• W2015142802 hasConcept C55493867 @default.
• W2015142802 hasConcept C62520636 @default.
• W2015142802 hasConcept C67705224 @default.
• W2015142802 hasConcept C8010536 @default.
• W2015142802 hasConcept C86803240 @default.
• W2015142802 hasConceptScore W2015142802C104317684 @default.
• W2015142802 hasConceptScore W2015142802C10879258 @default.
• W2015142802 hasConceptScore W2015142802C119599485 @default.
• W2015142802 hasConceptScore W2015142802C121332964 @default.
• W2015142802 hasConceptScore W2015142802C12554922 @default.
• W2015142802 hasConceptScore W2015142802C127413603 @default.
• W2015142802 hasConceptScore W2015142802C148898269 @default.
• W2015142802 hasConceptScore W2015142802C162203774 @default.
• W2015142802 hasConceptScore W2015142802C185592680 @default.
• W2015142802 hasConceptScore W2015142802C19472624 @default.
• W2015142802 hasConceptScore W2015142802C204328495 @default.
• W2015142802 hasConceptScore W2015142802C206276672 @default.
• W2015142802 hasConceptScore W2015142802C2776545253 @default.
• W2015142802 hasConceptScore W2015142802C55493867 @default.
• W2015142802 hasConceptScore W2015142802C62520636 @default.
• W2015142802 hasConceptScore W2015142802C67705224 @default.
• W2015142802 hasConceptScore W2015142802C8010536 @default.
• W2015142802 hasConceptScore W2015142802C86803240 @default.
• W2015142802 hasIssue "3" @default.
• W2015142802 hasLocation W20151428021 @default.
• W2015142802 hasLocation W20151428022 @default.
• W2015142802 hasOpenAccess W2015142802 @default.
• W2015142802 hasPrimaryLocation W20151428021 @default.
• W2015142802 hasRelatedWork W1981369098 @default.
• W2015142802 hasRelatedWork W2005625797 @default.
• W2015142802 hasRelatedWork W2018060167 @default.
• W2015142802 hasRelatedWork W2040362675 @default.
• W2015142802 hasRelatedWork W2089597488 @default.

• next