Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a

Journal Article · Tue Mar 21 04:00:00 EST 1989 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00432a008· OSTI ID:5546015

Zuiderweg, E R.P.; Fesik, S W ^[1]

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1. Abbott Laboratories, Abbott Park, IL (USA)

The utility of three-dimensional heteronuclear NMR spectroscopy for the assignment of {sup 1}H and {sup 15}N resonances of the inflammatory protein C5a (MW 8500), uniformly labeled with {sup 15}N, is demonstrated at a protein concentration of 0.7 mM. It is shown that dramatic simplification of the 2D nuclear Overhauser effect spectrum (NOESY) is obtained by editing with respect to the frequency of the {sup 15}N heteronucleus in a third dimension. The improved resolution in the 3D experiment largely facilitates the assignment of protein NMR spectra and allows for the determination of distance constraints from otherwise overlapping NOE cross peaks for purposes of 3D structure determination. The results show that {sup 15}N heteronuclear 3D NMR can facilitate the structure determination of small proteins and promises to be a useful tool for the study of larger systems that cannot be studied by conventional 2D NMR techniques.

• OSTI ID: 5546015
• Journal Information: Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 28:6; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
AQUEOUS SOLUTIONS
BARYONS
DISPERSIONS
ELEMENTARY PARTICLES
FERMIONS
HADRONS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MIXTURES
MOLECULAR STRUCTURE
NITROGEN 15
NITROGEN ISOTOPES
NUCLEAR MAGNETIC RESONANCE
NUCLEI
NUCLEONS
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
PROTEINS
PROTONS
RESONANCE
SOLUTIONS
STABLE ISOTOPES