Two‐dimensional 1H‐NMR studies of the solution structure of plasminogen kringle 4

Bridget C. MABBUTT, Robert J P WILLIAMS*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


Native kringle 4 from human plasminogen has been studied by two‐dimensional 1H‐NMR methods in order to obtain new structural information about the kringle fold. Two‐dimensional scalar correlated spectroscopy (COSY), two‐dimensional dipolar correlated spectroscopy (NOESY) and two‐dimensional relayed coherance transfer spectroscopy (RCT) experiments were recorded, allowing most resonances arising from the aromatic and methyl‐containing residues to be assigned in the spectrum. From an analysis of NOE data, a small segment of double‐stranded β‐sheet has been identified near residues Phe63 and Thr64. Further analysis of the NOESY spectrum has allowed detailed study of the conformation of sidechains located in regions near Leu45 and Val69. A model has been constructed of the polypeptide segment comprising residues 40–49 which accounts for the observed NOE interactions.

Original languageEnglish
Pages (from-to)539-548
Number of pages10
JournalEuropean Journal of Biochemistry
Issue number3
Publication statusPublished - 1988
Externally publishedYes


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