A proton magnetic relaxation study of methaemoproteins bound to monodisperse polystyrene latex particles

Bojan Benko; Stanimir Vuk-Pavlovic; Gjuro Dezelic; Sinisa Marićić

doi:10.1016/0021-9797(75)90269-6

A proton magnetic relaxation study of methaemoproteins bound to monodisperse polystyrene latex particles

Bojan Benko, Stanimir Vuk-Pavlovic, Gjuro Dezelic, Sinisa Marićić

Hematology

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	444-451
Number of pages	8
Journal	Journal of Colloid And Interface Science
Volume	52
Issue number	3
DOIs	https://doi.org/10.1016/0021-9797(75)90269-6
State	Published - Sep 1975

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Biomaterials
Surfaces, Coatings and Films
Colloid and Surface Chemistry

Access to Document

10.1016/0021-9797(75)90269-6

Fingerprint Dive into the research topics of 'A proton magnetic relaxation study of methaemoproteins bound to monodisperse polystyrene latex particles'. Together they form a unique fingerprint.

Cite this

@article{40aca3efc520458898d394be3ed32c38,

title = "A proton magnetic relaxation study of methaemoproteins bound to monodisperse polystyrene latex particles",

abstract = "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.",

author = "Bojan Benko and Stanimir Vuk-Pavlovic and Gjuro Dezelic and Sinisa Mari{\'c}i{\'c}",

year = "1975",

month = sep,

doi = "10.1016/0021-9797(75)90269-6",

language = "English (US)",

volume = "52",

pages = "444--451",

journal = "Journal of Colloid and Interface Science",

issn = "0021-9797",

publisher = "Academic Press Inc.",

number = "3",

}

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

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

VL - 52

SP - 444

EP - 451

JO - Journal of Colloid and Interface Science

JF - Journal of Colloid and Interface Science

SN - 0021-9797

IS - 3

ER -