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David A. Case
Researcher at Rutgers University
Publications - 369
Citations - 84216
David A. Case is an academic researcher from Rutgers University. The author has contributed to research in topics: Molecular dynamics & Solvation. The author has an hindex of 102, co-authored 364 publications receiving 74066 citations. Previous affiliations of David A. Case include University of Utah & Scripps Health.
Papers
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Journal ArticleDOI
Density Functional Calculations of Proton Chemical Shifts in Model Peptides
Doree Sitkoff,David A. Case +1 more
TL;DR: In this paper, density-functional chemical shielding calculations are reported for the alanine dipeptide with a variety of backbone torsion angles and for methane and N-methylacetamide complexes with rare gases, monatomic ions, water, and other amides.
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ff14ipq: A Self-Consistent Force Field for Condensed-Phase Simulations of Proteins
TL;DR: The ff14ipq model is an alternative to ff99SB and other Amber force fields for protein simulations in programs that accommodate pair-specific Lennard–Jones combining rules, and gives strong performance on α-helical and β-sheet oligopeptides as well as globular proteins over microsecond time scale simulations.
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X.alpha. multiple scattering calculations on copper porphine
David A. Case,Martin Karplus +1 more
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Observing reward-informative and -uninformative stimuli by normal children of different ages ☆
TL;DR: In this paper, normal children from ages 4 to 5, 9 to 10, and 13 to 14 years received points independent of responding according to a variable-time 30-sec schedule which alternated randomly with an extinction component.
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NMR solution structure of the inserted domain of human leukocyte function associated antigen-1.
Glen B. Legge,Richard W. Kriwacki,Josan Chung,Ulrich Hommel,Paul Ramage,David A. Case,H.J. Dyson,Peter E. Wright +7 more
TL;DR: The solution structure of the Mg(2+) complex of the I-domain of LFA-1 has been determined by NMR methods, using a model-based approach to nuclear Overhauser enhancement spectroscopy peak assignment and the role of divalent cations appears not to be as a direct mediator of a conformational change that alters affinity for the ligand.