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000056497 0247_ $$2DOI$$a10.1529/biophysj.106.094847
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000056497 084__ $$2WoS$$aBiophysics
000056497 1001_ $$0P:(DE-Juel1)VDB12272$$aHaber-Pohlmeier, S.$$b0$$uFZJ
000056497 245__ $$aBinding of Ca2+ to glutamic acid-rich polypeptides from the rod outer segment
000056497 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2007
000056497 300__ $$a3207 - 3214
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000056497 440_0 $$0882$$aBiophysical Journal$$v92$$x0006-3495
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000056497 520__ $$aRod photoreceptors contain three different glutamic acid-rich proteins (GARPs) that have been proposed to control the propagation of Ca(2+) from the site of its entry at the cyclic nucleotide-gated channel to the cytosol of the outer segment. We tested this hypothesis by measuring the binding of Ca(2+) to the following five constructs related to GARPs of rod photoreceptors: a 32-mer peptide containing 22 carboxylate groups, polyglutamic acid, a recombinant segment comprising 73 carboxylate groups (GLU), GARP1, and GARP2. Ca(2+) binding was investigated by means of a Ca(2+)-sensitive electrode. In all cases, Ca(2+) binds with low affinity; the half-maximum binding constant K(1/2) ranges from 6 to 16 mM. The binding stoichiometry between Ca(2+) ions and carboxylic groups is approximately 1:1; an exception is GARP2, where a binding stoichiometry of approximately 1:2 was found. Hydrodynamic radii of 1.6, 2.8, 3.3, 5.7, and 6.7 nm were determined by dynamic light scattering for the 32-mer, polyglutamic acid, GLU, GARP2, and GARP1 constructs, respectively. These results suggest that the peptides as well as GARP1 and GARP2 do not adopt compact globular structures. We conclude that the structures should be regarded as loose coils with low-affinity, high-capacity Ca(2+) binding.
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000056497 650_2 $$2MeSH$$aBinding Sites
000056497 650_2 $$2MeSH$$aCalcium: chemistry
000056497 650_2 $$2MeSH$$aGlutamic Acid: chemistry
000056497 650_2 $$2MeSH$$aNerve Tissue Proteins: chemistry
000056497 650_2 $$2MeSH$$aPeptides: chemistry
000056497 650_2 $$2MeSH$$aProtein Binding
000056497 650_2 $$2MeSH$$aRetinal Rod Photoreceptor Cells: chemistry
000056497 650_7 $$00$$2NLM Chemicals$$aNerve Tissue Proteins
000056497 650_7 $$00$$2NLM Chemicals$$aPeptides
000056497 650_7 $$056-86-0$$2NLM Chemicals$$aGlutamic Acid
000056497 650_7 $$07440-70-2$$2NLM Chemicals$$aCalcium
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000056497 7001_ $$0P:(DE-Juel1)VDB15797$$aAbarca Heidemann, K.$$b1$$uFZJ
000056497 7001_ $$0P:(DE-Juel1)VDB31218$$aKörschen, H. G.$$b2$$uFZJ
000056497 7001_ $$0P:(DE-HGF)0$$aKaur Dhiman, H.$$b3
000056497 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b4$$uFZJ
000056497 7001_ $$0P:(DE-HGF)0$$aSchwalbe, H.$$b5
000056497 7001_ $$0P:(DE-Juel1)VDB44599$$aKlein-Seetharaman, J.$$b6$$uFZJ
000056497 7001_ $$0P:(DE-Juel1)VDB728$$aKaupp, U. B.$$b7$$uFZJ
000056497 7001_ $$0P:(DE-Juel1)VDB1270$$aPohlmeier, A.$$b8$$uFZJ
000056497 773__ $$0PERI:(DE-600)1477214-0$$a10.1529/biophysj.106.094847$$gVol. 92, p. 3207 - 3214$$p3207 - 3214$$q92<3207 - 3214$$tBiophysical journal$$v92$$x0006-3495$$y2007
000056497 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1852358
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