Cathy C. Lester
Cornell University
7 Papers
75 Citations
Cathy C. Lester is an academic researcher from Cornell University. The author has contributed to research in topics: RNase P & Bovine pancreatic ribonuclease. The author has an hindex of 5, co-authored 7 publications.
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Papers
Retention of the cis proline conformation in tripeptide fragments of bovine pancreatic ribonuclease A containing a non-natural proline analogue, 5,5-dimethylproline
Seong Soo A. An,Cathy C. Lester,Jin-Lin Peng,Yue-Jin Li,David M. Rothwarf,Ervin Welker,Theodore W. Thannhauser,Lianshan Zhang,and James P. Tam,Harold A. Scheraga +9 more
TL;DR: In this article, the authors focused on l-5,5-dimethylproline (dmP) as a substitute to lock l-proline in a cis conformation in peptides and proteins, to prevent cis/trans isomerization when a protein with cis X-Pro peptide groups unfolds.
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A Caffeoylcyclohexane-1-Carboxylic Acid Derivative From Asimina Triloba
TL;DR: Three caffeoyl derivatives of 1,3,4,5-tetrahydroxycyclohexane 1-carboxylic acid were isolated from Asimina triloba and the structure of the active isomer, 3-caffeoyl- muco -quinic acid, was determined by extensive NMR studies.
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Elicited cell suspension cultures of apple (Malus × domestica) cv. Liberty produce biphenyl phytoalexins.
TL;DR: Yeast extract treated cell suspension cultures from a scab resistant apple cultivar, Malus×domestica cv.
31
New general approach for determining the solution structure of a ligand bound weakly to a receptor: structure of a fibrinogen Aalpha-like peptide bound to thrombin (S195A) obtained using NOE distance constraints and an ECEPP/3 flexible docking program.
TL;DR: Structural calculations of the bound ligand, using 2D‐transferred NOESY distance constraints in the DIANA program, showed that the N‐terminal portion of the peptide involves a chain reversal, whereas the C‐Terminal portion adopts a fold that exists in several different orientations.
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Regeneration studies of an analog of ribonuclease A missing disulfide bonds 65-72 and 40-95.
TL;DR: One-dimensional 1H NMR spectra demonstrated that the conformations of these three species are similar and are predominantly disordered; however, there is evidence of local structure in the vicinity of one histidine residue.
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