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Jack H. Freed

Researcher at Cornell University

Publications -  468
Citations -  24789

Jack H. Freed is an academic researcher from Cornell University. The author has contributed to research in topics: Electron paramagnetic resonance & Relaxation (NMR). The author has an hindex of 82, co-authored 459 publications receiving 23392 citations. Previous affiliations of Jack H. Freed include Dartmouth College & University of Freiburg.

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Conformational Dynamics in Extended RGD-Containing Peptides.

TL;DR: It is found that disorder of the binding site is important to the potency of RGD peptides, and that transient hydrogen bonding near the RGD site affects both the energy landscape roughness of the peptides and peptide binding.
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Deuterium NMR study of the structure and dynamic of the side chains of several solid polyglutamates

TL;DR: In this article, a /sup 2/H NMR study of polycrystalline powders and oriented films of several selectively deuterium-labeled poly(..gamma..-benzyl L-glutamate) (PBLG) and poly(.gamma,.-ethyl L-lglutamide) homopolymers is reported.
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Theory of Spin Relaxation via Quantum-Molecular Systems: Resonance Effects

TL;DR: In this article, a relaxation equation for the spin density matrix is derived on the assumptions that the spins are weakly coupled to the molecular degrees of freedom which are described quantum mechanically and the relaxation of the molecular systems is well represented by a general time-independent relaxation matrix which can include effects of weak as well as strong collisions.
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The internal dynamics of mini c TAR DNA probed by electron paramagnetic resonance of nitroxide spin-labels at the lower stem, the loop, and the bulge.

TL;DR: Electron paramagnetic resonance (EPR) at 236.6 and 9.5 GHz probed the tumbling of nitroxide spin probes in the lower stem, in the upper loop, and near the bulge of mini c TAR DNA, finding the slowing of nanosecond motions of large segments of the oligonucleotide was enhanced by increasing the ratio of the nucleocapsid protein NCp7 to mini cTAR DNA from 0 to 2.