Kenneth S. Rotondi, Ph.D. - Publications
Affiliations: | 2002 | University of Massachusetts, Amherst, Amherst, MA |
Area:
protein foldingYear | Citation | Score | |||
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2006 | Rotondi KS, Gierasch LM. Natural polypeptide scaffolds: beta-sheets, beta-turns, and beta-hairpins. Biopolymers. 84: 13-22. PMID 16235261 DOI: 10.1002/Bip.20390 | 0.631 | |||
2005 | Sinha N, Grant CV, Rotondi KS, Feduik-Rotondi L, Gierasch LM, Opella SJ. Peptides and the development of double- and triple-resonance solid-state NMR of aligned samples. The Journal of Peptide Research : Official Journal of the American Peptide Society. 65: 605-20. PMID 15885119 DOI: 10.1111/J.1399-3011.2005.00262.X | 0.433 | |||
2005 | Rotondi KS, Gierasch LM. A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution. Biopolymers. 80: 374-85. PMID 15815985 DOI: 10.1002/Bip.20238 | 0.539 | |||
2003 | Rotondi KS, Gierasch LM. Local sequence information in cellular retinoic acid-binding protein I: specific residue roles in beta-turns. Biopolymers. 71: 638-51. PMID 14991674 DOI: 10.1002/Bip.10592 | 0.678 | |||
2003 | Rotondi KS, Gierasch LM. Role of local sequence in the folding of cellular retinoic abinding protein I: structural propensities of reverse turns. Biochemistry. 42: 7976-85. PMID 12834350 DOI: 10.1021/Bi034304K | 0.664 | |||
2003 | Rotondi KS, Rotondi LF, Gierasch LM. Native structural propensity in cellular retinoic acid-binding protein I 64-88: the role of locally encoded structure in the folding of a beta-barrel protein. Biophysical Chemistry. 100: 421-36. PMID 12646381 DOI: 10.1016/S0301-4622(02)00296-X | 0.671 | |||
1997 | Clark PL, Sukumar M, Liu ZP, Rizo J, Rotondi K, Gierasch LM. Folding of a predominantly beta sheet protein with a central cavity Faseb Journal. 11: A871. | 0.609 | |||
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