Adhesion and clustering of charge isomers of myelin basic protein at model myelin membranesq

323 14 1147 1 3527 document 1147 SH1[1]-2003.pdf application/pdf 7ef9273b963c78a91a8a4bf3bffd3861 MD5 206942 2014-01-21 00:52:10 http://eprints.iliauni.edu.ge/323/1/SH1%5B1%5D-2003.pdf 323 1 1 application/pdf text ge public

SH1[1]-2003.pdf

1148 2 3538 document 1148 lightbox.jpg image/png 1b7e362ba527e05bfcbdd05ae49e83a0 MD5 54574 2014-01-21 01:12:12 http://eprints.iliauni.edu.ge/323/2/lightbox.jpg 323 2 2 image/png other Thumbnails conversion from text to thumbnail_lightbox ge public

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http://eprints.org/relation/isVersionOf http://eprints.iliauni.edu.ge/id/document/1147 http://eprints.org/relation/isVolatileVersionOf http://eprints.iliauni.edu.ge/id/document/1147 http://eprints.org/relation/issmallThumbnailVersionOf http://eprints.iliauni.edu.ge/id/document/1147 archive 61 disk0/00/00/03/23 2014-01-21 09:41:18 2015-04-21 12:35:09 2014-01-21 09:41:18 article show Shanshiashvili Lali lali_shanshiashvili@iliauni.edu.ge Suknidze N.Ch. Machaidze G.G. Mikeladze D.G. Ramsden J.J. Adhesion and clustering of charge isomers of myelin basic protein at model myelin membranesq pub QH301 RB RC0321 ins10 public The association of myelin basic protein charge isomers with the lipid part of the myelin membrane was investigated at the microscopic (molecular) level in a model membrane system, using optical waveguide lightmode spectrometry to determine with high precision the kinetics of association and dissociation to planar phospholipid membranes under controlled hydrodynamic conditions and over a range of protein concentrations. Detailed analysis of the data revealed a rich and intricate behaviour and clearly showed that the membrane protein affinity is characterized by at least four independent parameters: (i) the association rate coefficient characterizing the protein–membrane interaction energy as the protein approaches the fluid–membrane interface; (ii) the protein– membrane adhesion, i.e., the probability that it will remain at the membrane after arrival; (iii) the protein conformation at the membrane; and (iv) the protein�s tendency to cluster at the membrane. Some of these parameters varied in characteristic ways as the bulk solution concentration of the protein was varied, giving further clues to the detailed molecular comportment of the protein. The parameters and their characteristic variations with bulk concentration were markedly different for the different isomers. Implications of these results for neurological disorders involving demyelination, such as multiple sclerosis, are discussed. 2003 Archives of Biochemistry and Biophysics 419 ELSEVIER 170-177 10.1016/j.abb.2003.09.020 TRUE http://www.elsevier.com/locate/yabbi Supported by INTAS Grant No. 97-1561.