J
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.
Papers
More filters
Reference EntryDOI
Dipolar Spectroscopy – Single‐Resonance Methods
Peter P. Borbat,Jack H. Freed +1 more
Journal ArticleDOI
Dynamics and ordering of lipid spin-labels along the coexistence curve of two membrane phases: an ESR study.
Andrew K. Smith,Jack H. Freed +1 more
TL;DR: A molecular model of the L(o) phase is proposed incorporating the "condensing effect" of cholesterol on the phospholipid acyl chain dynamics and ordering and the “umbrella model” of the phosphoipid headgroup dynamics and order.
Journal ArticleDOI
On cooperative modes of reorientation in liquid crystals
Gary P. Zientara,Jack H. Freed +1 more
TL;DR: In this article, the role of cooperative modes of reorientation in liquid crystals for the spectral densities of importance in magnetic resonance relaxation is examined from the viewpoint of microscopic models that can be solved analytically.
Journal ArticleDOI
Backbone dynamics of deoxy and carbonmonoxy hemoglobin by NMR/SRLS.
TL;DR: The slowly relaxing local structure (SRLS) approach, developed for NMR spin relaxation analysis in proteins, is applied herein to amide ¹⁵N relaxation in deoxy and carbonmonoxy hemoglobin to provide physical clarity, inherent potential for further interpretation, consistency, and new qualitative insights provided.
Journal ArticleDOI
Site-Specific Incorporation of a Cu2+ Spin Label into Proteins for Measuring Distances by Pulsed Dipolar Electron Spin Resonance Spectroscopy.
Gregory E. Merz,Peter P. Borbat,Alise Muok,Madhur Srivastava,David N. Bunck,Jack H. Freed,Brian R. Crane +6 more
TL;DR: Site-specific incorporation of Cu2+ into non-metalloproteins through the use of a genetically encodable non-natural amino acid, 3-pyrazolyltyrosine, is demonstrated and PDS measurements of CheY-PyTyr with nitroxide-labeled CheA provide new insights into the conformational landscape of the phosphotransfer complex.