Nuclear Magnetic Resonance Studies of Proteins

NUCLEAR MAGNETIC RESONANCE STUDY OF THE STRUCTURE OF GLYOXALDIHYDRAZONE

Study of the nuclear magnetic resonance spectra of glyoxaldihydrazone in dimethylsulfoxide and deuterochlorofonn leads to the conclusion that this compound exists predominantly in non-chelate structure

Nuclear Magnetic Resonance Studies of Rotational Correlation Times of Proteins Resonance Spectroscopy+

We show that measurement of the spin-lattice ( T I ) and spin-spin ( Tz) relaxation times (or line widths) of irrotationally bound 2H nuclei in macromolecules undergoing isotropic rotational motion outside of the extreme narrowing limit (Le., for the case W o ’ 7 ~ ~ >> 1) permits determination of both the rotational correlation time ( T R ) of the macromolecule and the electric quadrupole coup...

Nuclear magnetic resonance studies of allergens.

Nuclear magnetic resonance studies of phospholipid micelles.

The proton magnetic resonance spectrum of DL-a!-lecithin at 100 MHz in CHCJ solvent is reported. An analysis of the spectrum is made. The chemical shifts of the N-(CH& protons and the resonance peak associated with the condensed water molecule showed concentration dependence with the latter showing the more pronounced response. These chemical shift changes are interpreted in terms of micelle fo...

Structural studies of large integral membrane proteins in reverse micelles by solution nuclear magnetic resonance

The structural characterization of integral membrane proteins represents one of the many challenges of the post-genomic era. While membrane proteins comprise approximately 50% of current and potential drug targets, their structural characterization lags far behind that of soluble proteins. Nuclear magnetic resonance (NMR) offers tremendous potential for the investigation of membrane proteins in...