TY - JOUR
T1 - Two‐dimensional 1H‐NMR studies of the solution structure of plasminogen kringle 4
AU - MABBUTT, Bridget C.
AU - WILLIAMS, Robert J P
PY - 1988
Y1 - 1988
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0023818904&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1988.tb13733.x
DO - 10.1111/j.1432-1033.1988.tb13733.x
M3 - Article
C2 - 3338450
AN - SCOPUS:0023818904
SN - 0014-2956
VL - 170
SP - 539
EP - 548
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 3
ER -