TY - JOUR
T1 - A proton magnetic relaxation study of methaemoproteins bound to monodisperse polystyrene latex particles
AU - Benko, Bojan
AU - Vuk-Pavlovic, Stanimir
AU - Dezelic, Gjuro
AU - Marićić, Sinisa
N1 - Funding Information:
This work was carried out under the PL-480 contract No. 02-004-1 between the N.I.H. (U.S.A.) and The Institute of Biology, University of Zagreb, with the partial support of the Research Fund of the S. R. Croatia. The first two authors thank the latter Fund and The Institute of Biology for postgraduate scholarships. Part of this work has been submitted by the
PY - 1975/9
Y1 - 1975/9
N2 - The influence of the binding of methaemoproteins to latex particles with respect to protein conformation was examined using the longitudinal magnetic relaxation rates of solvent protons. The temperature dependences of the paramagnetically induced molar relaxation rates in bound metmyoglobin samples as well as their absolute values suggest an opening of the haem-pocket. The decrease of the same parameter for the immobilized methaemoglobin points to a smaller haem-pocket accessibility with respect to that in the solution. The changes of the haem-pocket structure found for both methaemoproteins support the idea that proteins change their conformation by their binding to the solid surface, although in opposite ways.
AB - The influence of the binding of methaemoproteins to latex particles with respect to protein conformation was examined using the longitudinal magnetic relaxation rates of solvent protons. The temperature dependences of the paramagnetically induced molar relaxation rates in bound metmyoglobin samples as well as their absolute values suggest an opening of the haem-pocket. The decrease of the same parameter for the immobilized methaemoglobin points to a smaller haem-pocket accessibility with respect to that in the solution. The changes of the haem-pocket structure found for both methaemoproteins support the idea that proteins change their conformation by their binding to the solid surface, although in opposite ways.
UR - http://www.scopus.com/inward/record.url?scp=3042589512&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=3042589512&partnerID=8YFLogxK
U2 - 10.1016/0021-9797(75)90269-6
DO - 10.1016/0021-9797(75)90269-6
M3 - Article
AN - SCOPUS:3042589512
SN - 0021-9797
VL - 52
SP - 444
EP - 451
JO - Journal of Colloid And Interface Science
JF - Journal of Colloid And Interface Science
IS - 3
ER -