PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 11895078

Multidimensional NMR methods for protein structure determination.

V Kanelis·J D Forman-Kay·L E Kay
View original source ↗Export metadata ↓

Abstract

Structural studies of proteins are critical for understanding biological processes at the molecular level. Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for obtaining structural and dynamic information on proteins and protein-ligand complexes. In the present review, methodologies for NMR structure determination of proteins and macromolecular complexes are described. In addition, a number of recent advances that reduce the molecular weight limitations previously imposed on NMR studies of biomolecules are discussed, highlighting applications of these technologies to protein systems studied in our laboratories.

Explore related subjects

Magnetic Resonance SpectroscopyModels, ChemicalModels, MolecularProtein ConformationProteinsSpectrum AnalysisJournal ArticleResearch Support, Non-U.S. Gov'tReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

V Kanelis, J D Forman-Kay, L E Kay. 2001. Multidimensional NMR methods for protein structure determination.. https://doi.org/10.1080/152165401317291147

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2003

Total diastereofacial selective iodofunctionalization of terpene derivatives based on Ipy2BF4.

Acetonides 1, easily obtained from simple terpenes, react with bispyridine iodonium (I) tetrafluoroborate (Ipy(2)BF(4)) and tetrafluoroboric acid in the presence of nucleophiles to give the corresponding adducts 2 with complete regio and diastereofacial control. Acetonides 1 containing a properly located phenyl or benzyloxy group easily undergo iodocyclization to furnish compounds 3 and 4.

Magnetic Resonance Spectroscopy↗
PubMed2003

Increase in signal-to-noise ratio of > 10,000 times in liquid-state NMR.

A method for obtaining strongly polarized nuclear spins in solution has been developed. The method uses low temperature, high magnetic field, and dynamic nuclear polarization (DNP) to strongly polarize nuclear spins in the solid state. The solid sample is subsequently dissolved rapidly in a suitable solvent to create a solution of molecules with hyperpolarized nuclear spins. The polarization is performed in a DNP polarizer, consisting of a super-conducting magnet (3.35 T) and a liquid-helium cooled sample space. The sample is irradiated with microwaves at approximately 94 GHz. Subsequent to polarization, the sample is dissolved by an injection system inside the DNP magnet. The dissolution process effectively preserves the nuclear polarization. The resulting hyperpolarized liquid sample can be transferred to a high-resolution NMR spectrometer, where an enhanced NMR signal can be acquired, or it may be used as an agent for in vivo imaging or spectroscopy. In this article we describe the use of the method on aqueous solutions of [13C]urea. Polarizations of 37% for 13C and 7.8% for 15N, respectively, were obtained after the dissolution. These polarizations correspond to an enhancement of 44,400 for 13C and 23,500 for 15N, respectively, compared with thermal equilibrium at 9.4 T and room temperature. The method can be used generally for signal enhancement and reduction of measurement time in liquid-state NMR and opens up for a variety of in vitro and in vivo applications of DNP-enhanced NMR.

Magnetic Resonance Spectroscopy↗
PubMed2003

Calyciphyllines A and B, two novel hexacyclic alkaloids from Daphniphyllum calycinum.

[structure: see text] Two types of Daphniphyllum alkaloids with unprecedented fused-hexacyclic ring systems, calyciphyllines A (1) and B (2), have been isolated from the leaves of Daphniphyllum calycinum (Daphniphyllaceae), and the structures and relative stereochemistry were elucidated on the basis of spectroscopic data.

Magnetic Resonance Spectroscopy↗