Arnold C. Satterthwait
Scripps Research Institute
26 Papers
500 Citations
Arnold C. Satterthwait is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Metaphosphate & Peptide. The author has an hindex of 15, co-authored 26 publications.
Chat about Author
Papers
Molecular profile of an antibody response to HIV-1 as probed by combinatorial libraries
Carlos F. Barbas,Thomas A. Collet,Willi Amberg,Paul Roben,James M. Binley,Denise M. Hoekstra,Doug Cababa,Terri Jones,R. Anthony Williamson,Glenn R. Pilkington,Nancy L. Haigwood,Edelmira Cabezas,Arnold C. Satterthwait,Iñaki Sanz,Dennis R. Burton +14 more
TL;DR: A large number (33) of human Fab fragments reacting with HIV-1 surface glycoprotein gp120 have been generated by selection from a combinatorial IgG1 kappa library displayed on the surface of phage.
261
The Hydrogen Bond Mimic Approach: Solid-Phase Synthesis of a Peptide Stabilized as an α-Helix with a Hydrazone Link
TL;DR: In this article, a solid-phase synthesis for replacing a main-chain hydrogen bond (NH → OCRNH) with a hydrazone link (N−NCH−CH2CH2) in peptides is described.
165
Dual conformations for the HIV-1 gp120 V3 loop in complexes with different neutralizing Fabs
Robyn L. Stanfield,Edelmira Cabezas,Arnold C. Satterthwait,Enrico A. Stura,Albert T. Profy,Ian A. Wilson +5 more
TL;DR: The V3 loop of HIV-1 gp120 can adopt at least two different conformations for the highly conserved Gly-Pro-Gly-Arg sequence at the tip of the loop, suggesting some inherent conformational flexibility that may relate to its biological function.
127
Structure-based design of a constrained peptide mimic of the HIV-1 V3 loop neutralization site.
TL;DR: Proton nuclear magnetic resonance studies indicate that the free Aib142 peptide is indeed more ordered in solution with a conformational preference that corresponds to the X-ray structure of its Fab-bound form, and represents the first step in the design of conformationally constrained peptide analogs built to mimic biologically relevant structural forms of HIV-1 neutralization sites.
79