FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2066734465> ?p ?o ?g. }

• W2066734465 endingPage "109" @default.
• W2066734465 startingPage "96" @default.
• W2066734465 abstract "Aggregation in the brain of polyglutamine-containing proteins is either a cause or an associated symptom of nine hereditary neurodegenerative disorders including Huntington's disease. The molecular level mechanisms by which these proteins aggregate are still unclear. In an effort to shed light on this important phenomenon, we are investigating the aggregation of model polyglutamine peptides using molecular-level computer simulation with a simplified model of polyglutamine that we have developed. This model accounts for the most important types of intra- and inter-molecular interactions-hydrogen bonding and hydrophobic interactions-while allowing the folding process to be simulated in a reasonable time frame. The model is used to examine the folding of isolated polyglutamine peptides 16, 32, and 48 residues long and the folding and aggregation of systems of 24 model polyglutamine peptides 16, 24, 32, 36, 40, and 48 residues long. Although the isolated polyglutamine peptides did form some alpha and beta backbone-backbone hydrogen bonds they did not have as many of these bonds as they would have if they had folded into a complete alpha helix or beta sheet. In one of the simulations on the isolated polyglutamine peptide 48 residues long, we observed a structure that resembles a beta helix. In the multi-chain simulations we observed amorphous aggregates at low temperatures, ordered aggregates with significant beta sheet character at intermediate temperatures, and random coils at high temperatures. We have found that the temperature at which the model peptides undergo the transition from amorphous aggregates to ordered aggregates and the temperature at which the model peptides undergo the transition from ordered aggregates to random coils increase with increasing chain length. Our finding that the stability of the ordered aggregates increases as the peptide chain length increases may help to explain the experimentally observed relation between polyglutamine tract length and aggregation in vitro and disease progression in vivo. We have also observed in our simulations that the optimal temperature for the formation of beta sheets increases with chain length up to 36 glutamine residues but not beyond. Equivalently, at fixed temperature we find a transition from a region dominated by random coils at chain lengths less than 36 to a region dominated by relatively ordered beta sheet structures at chain lengths greater than 36. Our finding of this critical chain length of 36 glutamine residues is interesting because a critical chain length of 37 glutamine residues has been observed experimentally." @default.
• W2066734465 created "2016-06-24" @default.
• W2066734465 creator A5054651695 @default.
• W2066734465 creator A5057051008 @default.
• W2066734465 date "2006-10-26" @default.
• W2066734465 modified "2023-10-09" @default.
• W2066734465 title "Effects of chain length on the aggregation of model polyglutamine peptides: Molecular dynamics simulations" @default.
• W2066734465 cites W1968509832 @default.
• W2066734465 cites W1986982278 @default.
• W2066734465 cites W1988760238 @default.
• W2066734465 cites W1989619236 @default.
• W2066734465 cites W1992453786 @default.
• W2066734465 cites W1992874118 @default.
• W2066734465 cites W1995462290 @default.
• W2066734465 cites W1995931393 @default.
• W2066734465 cites W1996667889 @default.
• W2066734465 cites W1996789718 @default.
• W2066734465 cites W2001599007 @default.
• W2066734465 cites W2002368654 @default.
• W2066734465 cites W2008307658 @default.
• W2066734465 cites W2012481532 @default.
• W2066734465 cites W2013011381 @default.
• W2066734465 cites W2016881055 @default.
• W2066734465 cites W2017268899 @default.
• W2066734465 cites W2018632557 @default.
• W2066734465 cites W2023067664 @default.
• W2066734465 cites W2027581523 @default.
• W2066734465 cites W2027594237 @default.
• W2066734465 cites W2029430054 @default.
• W2066734465 cites W2031119375 @default.
• W2066734465 cites W2032255653 @default.
• W2066734465 cites W2034160988 @default.
• W2066734465 cites W2036142355 @default.
• W2066734465 cites W2039491234 @default.
• W2066734465 cites W2039516928 @default.
• W2066734465 cites W2041993377 @default.
• W2066734465 cites W2043899474 @default.
• W2066734465 cites W2048221161 @default.
• W2066734465 cites W2048339661 @default.
• W2066734465 cites W2055188598 @default.
• W2066734465 cites W2055680113 @default.
• W2066734465 cites W2057158394 @default.
• W2066734465 cites W2058543711 @default.
• W2066734465 cites W2064551580 @default.
• W2066734465 cites W2065248623 @default.
• W2066734465 cites W2066604274 @default.
• W2066734465 cites W2067644428 @default.
• W2066734465 cites W2069607465 @default.
• W2066734465 cites W2070422126 @default.
• W2066734465 cites W2070795929 @default.
• W2066734465 cites W2071677894 @default.
• W2066734465 cites W2072287157 @default.
• W2066734465 cites W2073012734 @default.
• W2066734465 cites W2073886687 @default.
• W2066734465 cites W2074182100 @default.
• W2066734465 cites W2074255526 @default.
• W2066734465 cites W2079250951 @default.
• W2066734465 cites W2079547500 @default.
• W2066734465 cites W2085899859 @default.
• W2066734465 cites W2088599251 @default.
• W2066734465 cites W2088661320 @default.
• W2066734465 cites W2089386161 @default.
• W2066734465 cites W2090771452 @default.
• W2066734465 cites W2091441518 @default.
• W2066734465 cites W2095151479 @default.
• W2066734465 cites W2099997349 @default.
• W2066734465 cites W2104306407 @default.
• W2066734465 cites W2104650717 @default.
• W2066734465 cites W2110515879 @default.
• W2066734465 cites W2114068476 @default.
• W2066734465 cites W2119210227 @default.
• W2066734465 cites W2120531463 @default.
• W2066734465 cites W2121642311 @default.
• W2066734465 cites W2122495582 @default.
• W2066734465 cites W2123231783 @default.
• W2066734465 cites W2124929769 @default.
• W2066734465 cites W2133272695 @default.
• W2066734465 cites W2137261793 @default.
• W2066734465 cites W2137374371 @default.
• W2066734465 cites W2138854816 @default.
• W2066734465 cites W2140112946 @default.
• W2066734465 cites W2140797187 @default.
• W2066734465 cites W2146462263 @default.
• W2066734465 cites W2147251458 @default.
• W2066734465 cites W2148963049 @default.
• W2066734465 cites W2150464190 @default.
• W2066734465 cites W2157208586 @default.
• W2066734465 cites W2168715581 @default.
• W2066734465 cites W2170168709 @default.
• W2066734465 cites W2170998869 @default.
• W2066734465 cites W2171705617 @default.
• W2066734465 cites W2255469197 @default.
• W2066734465 cites W4232338625 @default.
• W2066734465 cites W4244779656 @default.
• W2066734465 cites W4383673615 @default.
• W2066734465 doi "https://doi.org/10.1002/prot.21132" @default.
• W2066734465 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17068817" @default.
• W2066734465 hasPublicationYear "2006" @default.

• next