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Solution studies of staphylococcal nuclease H124L. 1. Backbone sup 1 H and sup 15 N resonances and secondary structure of the unligated enzyme as identified by three-dimensional NMR spectroscopy

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00118a038· OSTI ID:5488849
; ; ;  [1]
  1. Univ. of Wisconsin, Madison (United States)
+ Show Author Affiliations
The backbone {sup 1}H and {sup 15}N resonances of unligated staphylococcal nuclease H124L (recombinant protein produced in Escherichia coli whose sequence is identical to the nuclease produced by the V8 strain of Staphylococcus aureus) have been assigned by three-dimensional (3D) {sup 1}H-{sup 15}N NOESY-HMQC NMR spectroscopy at 14.1 tesla. The protein sample used in this study was labeled uniformly with {sup 15}N to a level greater than 95% by growing the E. coli host on a medium containing (99% {sup 15}N)ammonium sulfate as the sole nitrogen source. The assignments include 82% of the backbone {sup 1}H{sup N} and {sup 1}H{sup {alpha}} resonances as well as the {sup 15}N resonances of non-proline residues. Secondary structural elements ({alpha}-helices, {beta}-sheets, reverse turns, and loops) were determined by analysis of patterns of NOE connectivities present in the 3D spectrum.
OSTI ID:
5488849
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 31:3; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English

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Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AQUEOUS SOLUTIONS
BACTERIA
BARYONS
DISPERSIONS
ELEMENTARY PARTICLES
ENZYMES
ESCHERICHIA COLI
ESTERASES
FERMIONS
HADRONS
HYDROLASES
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MICROORGANISMS
MIXTURES
NITROGEN 15
NITROGEN ISOTOPES
NUCLEAR MAGNETIC RESONANCE
NUCLEASES
NUCLEI
NUCLEONS
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
PHOSPHODIESTERASES
PROTEINS
PROTONS
RESONANCE
SOLUTIONS
STABLE ISOTOPES
STAPHYLOCOCCUS