T
Trevor P. Creamer
Researcher at University of Kentucky
Publications - 56
Citations - 4452
Trevor P. Creamer is an academic researcher from University of Kentucky. The author has contributed to research in topics: Polyproline helix & Calmodulin. The author has an hindex of 30, co-authored 55 publications receiving 4201 citations. Previous affiliations of Trevor P. Creamer include Washington University in St. Louis & Johns Hopkins University School of Medicine.
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Journal ArticleDOI
Solvation Energies of Amino Acid Side Chains and Backbone in a Family of Host−Guest Pentapeptides
TL;DR: The very large peptide bond ASP, -96 +/- 6 cal/mol/A2, profoundly affects the results of computational comparisons of protein stability which use ASPs derived from octanol-water partitioning data.
Journal ArticleDOI
Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism
Ashwani Kumar Thakur,Murali Jayaraman,Rakesh Mishra,Monika Thakur,Veronique M. Chellgren,In-Ja L. Byeon,Dalaver H. Anjum,Ravindra Kodali,Trevor P. Creamer,James F. Conway,Angela M. Gronenborn,Ronald Wetzel +11 more
TL;DR: It is shown that the 17-amino-acid flanking sequence N-terminal to the polyQ in the toxic huntingtin exon 1 fragment imparts onto this peptide a complex alternative aggregation mechanism that greatly enhances its aggregation into globular oligomers with HTTNT cores and exposed polyQ.
Journal ArticleDOI
Side-Chain Entropy Opposes |alpha-Helix Formation but Rationalizes Experimentally Determined Helix-Forming Propensities
TL;DR: The results indicate that the drive to form helices must originate in the backbone, consistent with Pauling's view of four decades ago.
Journal ArticleDOI
Oligoproline effects on polyglutamine conformation and aggregation.
Anusri M. Bhattacharyya,Ashwani Kumar Thakur,Veronique M. Chellgren,Geetha Thiagarajan,Angela Williams,Brian W. Chellgren,Trevor P. Creamer,Ronald Wetzel +7 more
TL;DR: It is shown here that introduction of a P10 sequence C-terminal to polyGln in synthetic peptides decreases both the rate of formation and the apparent stability of the amyloid-like aggregates associated with Huntington's disease.
Journal ArticleDOI
A survey of left-handed polyproline II helices.
TL;DR: A survey of 274 nonhomologous polypeptide chains from proteins of known structure for regions that form these structures finds significant correlation between the hydrophobicity of residues at i and i + 3; thus, PPII helices in globular proteins can be considered to be amphipathic.