Publication Date:
1988-05-13
Description:
By applying a two-dimensional double-quantum carbon-13 nuclear magnetic resonance experiment to a protein uniformly enriched to 26 percent carbon-13, networks of directly bonded carbon atoms were identified by virtue of their one-bond spin-spin couplings and were classified by amino acid type according to their particular single- and double-quantum chemical shift patterns. Spin systems of 75 of the 98 amino acid residues in a protein, oxidized Anabaena 7120 ferredoxin (molecular weight 11,000), were identified by this approach, which represents a key step in an improved methodology for assigning protein nuclear magnetic resonance spectra. Missing spin systems corresponded primarily to residues located adjacent to the paramagnetic iron-sulfur cluster.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oh, B H -- Westler, W M -- Darba, P -- Markley, J L -- RR02301/RR/NCRR NIH HHS/ -- RR02781/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1988 May 13;240(4854):908-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3129784" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acids
;
Carbon Isotopes
;
Cyanobacteria/analysis
;
*Ferredoxins
;
*Magnetic Resonance Spectroscopy
;
Oxidation-Reduction
;
Spectrum Analysis
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
