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Isotope-detected /sup 1/H NMR studies of proteins: a general strategy for editing interproton nuclear Overhauser effects by heteronuclear decoupling, with application to phage lambda repressor

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)
; ;

A strategy for editing interproton nuclear Overhauser effects (NOEs) in proteins is proposed and illustrated. Selective incorporation of /sup 13/C- (or /sup 15/N)-labeled amino acids into a protein permits NOEs involving the labeled residues to be identified by heteronuclear difference decoupling. Such heteronuclear editing simplifies the NOE difference spectrum and avoids ambiguities due to spin diffusion. Isotope-detected /sup 1/H NMR thus opens to study proteins too large for conventional one- and two-dimensional NMR methods (20-75 kDa). The authors have applied this strategy to the N-terminal domain of phage lambda repressor, a protein of dimer molecular mass 23 kDa. A tertiary NOE from an internal aromatic ring (Phe-51) to a ..beta..-/sup 13/C-labeled alanine residue (Ala-62) is demonstrated.

Research Organization:
Harvard Univ., Cambridge, MA
OSTI ID:
5559180
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 83:5; ISSN PNASA
Country of Publication:
United States
Language:
English

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Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
ALANINES
AMINO ACIDS
BACTERIA
BACTERIOPHAGES
BARYONS
CARBON 13
CARBON ISOTOPES
CARBOXYLIC ACIDS
ELEMENTARY PARTICLES
ESCHERICHIA COLI
EVEN-ODD NUCLEI
FERMIONS
GENE REPRESSORS
HADRONS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MICROORGANISMS
MOLECULAR STRUCTURE
NITROGEN 15
NITROGEN ISOTOPES
NUCLEAR MAGNETIC RESONANCE
NUCLEI
NUCLEONS
NUCLEOPROTEINS
ODD-EVEN NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
PARASITES
PROTEINS
PROTONS
RESONANCE
STABLE ISOTOPES
VIRUSES