FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1977704740> ?p ?o ?g. }

• W1977704740 endingPage "1283" @default.
• W1977704740 startingPage "1267" @default.
• W1977704740 abstract "Conformational ensembles of fully disordered natural polypeptides represent the starting point of protein refolding initiated by transfer to folding conditions. Thus, understanding the transient properties and dimensions of such peptides under folding conditions is a necessary step in the understanding of their subsequent folding behavior. Such ensembles can also undergo alternative folding and form amyloid structures, which are involved in many neurological degenerative diseases. Here, we performed a structural study of this initial state using time-resolved fluorescence resonance energy transfer analysis of a series of eight partially overlapping double-labeled chain segments of the N-terminal and NAC domains of the α-synuclein molecule. The distributions of end-to-end distance and segmental intramolecular diffusion coefficients were simultaneously determined for eight labeled chain segments. We used the coefficient of variation, C(v), as a measure of the conformational heterogeneity (i.e., structural disorder). With the exception of two segments, the C(v)s were characteristic of a fully disordered state of the chain. Subtle deviations from this behavior at the segment labeled in the NAC domain and the segment at the N termini reflected subtle conformational bias that might be related to the initiation of transition to amyloid aggregates. The chain length dependence of the mean segmental end-to-end distance followed a power law as predicted by Flory, but the dependence was steeper than previously predicted, probably due to the contribution of the excluded volume effect, which is more dominant for shorter-chain segments. The observed intramolecular diffusion coefficients (<10 to ∼25 Ǻ(2)/ns) are only an order of magnitude lower than the common diffusion coefficients of low molecular weight probes. This diffusion coefficient increased with chain length, probably due to the cumulative contributions of minor bond rotations along the chain. These results gave us a reference both for characteristics of a natural unfolded polypeptide at the moment of initiation of folding and for detection of possible initiation sites of the amyloid transition." @default.
• W1977704740 created "2016-06-24" @default.
• W1977704740 creator A5040695867 @default.
• W1977704740 creator A5082572644 @default.
• W1977704740 date "2011-02-01" @default.
• W1977704740 modified "2023-09-27" @default.
• W1977704740 title "Segmental Conformational Disorder and Dynamics in the Intrinsically Disordered Protein α-Synuclein and Its Chain Length Dependence" @default.
• W1977704740 cites W1485449426 @default.
• W1977704740 cites W1515255916 @default.
• W1977704740 cites W1580614613 @default.
• W1977704740 cites W1965778124 @default.
• W1977704740 cites W1966130903 @default.
• W1977704740 cites W1968942251 @default.
• W1977704740 cites W1969163423 @default.
• W1977704740 cites W1969178181 @default.
• W1977704740 cites W1971389338 @default.
• W1977704740 cites W1973897761 @default.
• W1977704740 cites W1976660933 @default.
• W1977704740 cites W1976959587 @default.
• W1977704740 cites W1982663316 @default.
• W1977704740 cites W1983508666 @default.
• W1977704740 cites W1985277612 @default.
• W1977704740 cites W1988624456 @default.
• W1977704740 cites W1993145018 @default.
• W1977704740 cites W1996518756 @default.
• W1977704740 cites W1999599191 @default.
• W1977704740 cites W2001509033 @default.
• W1977704740 cites W2004291898 @default.
• W1977704740 cites W2006192061 @default.
• W1977704740 cites W2007419082 @default.
• W1977704740 cites W2009556855 @default.
• W1977704740 cites W2009890105 @default.
• W1977704740 cites W2010631370 @default.
• W1977704740 cites W2014337953 @default.
• W1977704740 cites W2016170088 @default.
• W1977704740 cites W2021977313 @default.
• W1977704740 cites W2027525036 @default.
• W1977704740 cites W2030447262 @default.
• W1977704740 cites W2036423396 @default.
• W1977704740 cites W2037410278 @default.
• W1977704740 cites W2043297959 @default.
• W1977704740 cites W2047138766 @default.
• W1977704740 cites W2049769943 @default.
• W1977704740 cites W2053203978 @default.
• W1977704740 cites W2054675545 @default.
• W1977704740 cites W2054737424 @default.
• W1977704740 cites W2060328944 @default.
• W1977704740 cites W2060745831 @default.
• W1977704740 cites W2066041565 @default.
• W1977704740 cites W2068898686 @default.
• W1977704740 cites W2071020344 @default.
• W1977704740 cites W2073745520 @default.
• W1977704740 cites W2076498192 @default.
• W1977704740 cites W2080751623 @default.
• W1977704740 cites W2084104753 @default.
• W1977704740 cites W2085987859 @default.
• W1977704740 cites W2087735191 @default.
• W1977704740 cites W2088481573 @default.
• W1977704740 cites W2088579293 @default.
• W1977704740 cites W2091265794 @default.
• W1977704740 cites W2092153867 @default.
• W1977704740 cites W2092206441 @default.
• W1977704740 cites W2092318974 @default.
• W1977704740 cites W2092356013 @default.
• W1977704740 cites W2092968558 @default.
• W1977704740 cites W2104017463 @default.
• W1977704740 cites W2104400769 @default.
• W1977704740 cites W2110113231 @default.
• W1977704740 cites W2114304598 @default.
• W1977704740 cites W2118608964 @default.
• W1977704740 cites W2131041114 @default.
• W1977704740 cites W2132595034 @default.
• W1977704740 cites W2144737808 @default.
• W1977704740 cites W2148225540 @default.
• W1977704740 cites W2149320847 @default.
• W1977704740 cites W2150656456 @default.
• W1977704740 cites W2156262248 @default.
• W1977704740 cites W2158977717 @default.
• W1977704740 cites W2180204534 @default.
• W1977704740 cites W2318393294 @default.
• W1977704740 cites W4210968583 @default.
• W1977704740 cites W4211239749 @default.
• W1977704740 cites W4246442978 @default.
• W1977704740 cites W4250968818 @default.
• W1977704740 doi "https://doi.org/10.1016/j.jmb.2010.11.011" @default.
• W1977704740 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21108951" @default.
• W1977704740 hasPublicationYear "2011" @default.
• W1977704740 type Work @default.
• W1977704740 sameAs 1977704740 @default.
• W1977704740 citedByCount "60" @default.
• W1977704740 countsByYear W19777047402012 @default.
• W1977704740 countsByYear W19777047402013 @default.
• W1977704740 countsByYear W19777047402014 @default.
• W1977704740 countsByYear W19777047402015 @default.
• W1977704740 countsByYear W19777047402016 @default.
• W1977704740 countsByYear W19777047402017 @default.
• W1977704740 countsByYear W19777047402018 @default.
• W1977704740 countsByYear W19777047402019 @default.

• next