K
Karunakar Kar
Researcher at Jawaharlal Nehru University
Publications - 48
Citations - 1790
Karunakar Kar is an academic researcher from Jawaharlal Nehru University. The author has contributed to research in topics: Amyloid & Protein aggregation. The author has an hindex of 22, co-authored 42 publications receiving 1480 citations. Previous affiliations of Karunakar Kar include Indian Institute of Technology, Jodhpur & Rutgers University.
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Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent
TL;DR: It is shown that over a short range of repeat lengths, from Q23 to Q26, the size of the critical nucleus for aggregation increases from monomeric to dimeric to tetrameric, and this variation in nucleus size suggests a common duplex antiparallel β-sheet framework for the nucleus.
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Triple-helical peptides: An approach to collagen conformation, stability, and self-association
TL;DR: The dependence of collagen triple-helix stability on the residues in its (Gly-X-Y)(n) repeating sequence has been investigated by measuring melting temperatures of host-guest peptides and an on-line collagen stability calculator is now available.
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Huntingtin exon 1 fibrils feature an interdigitated β-hairpin–based polyglutamine core
Cody L. Hoop,Hsiang Kai Lin,Karunakar Kar,Gábor Magyarfalvi,Jonathan M. Lamley,Jennifer C. Boatz,Abhishek Mandal,Józef R. Lewandowski,Ronald Wetzel,Patrick C.A. van der Wel +9 more
TL;DR: It is shown that the aggregation of mutant huntingtin exon1 proceeds via an intramolecular collapse of the expanded polyglutamine domain and the implications of this observation for understanding of its misfolding and aggregation mechanisms are discussed.
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Self-association of collagen triple helic peptides into higher order structures.
Karunakar Kar,Priyal Amin,Michael A. Bryan,Anton V. Persikov,Angela Mohs,Yuh-Hwa Wang,Barbara Brodsky +6 more
TL;DR: The triple helical form of (Pro-Hyp-Gly)10, a peptide that has proved a useful model for molecular features of collagen, was found to self-associate, and its association properties are reported here.
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Aromatic Interactions Promote Self-Association of Collagen Triple-Helical Peptides to Higher-Order Structures
TL;DR: It is suggested that the catalysis of type I collagen fibrillogenesis by nonhelical telopeptides is due to specific intermolecular CH...pi interactions between aromatic residues in the telopePTides and Pro/Hyp residues within the triple helix.