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• W2020009604 abstract "We used SpαI-1−156 peptide, a well-characterized model peptide of the αN-terminal region of erythrocyte spectrin, and SpαII-1−149, an αII brain spectrin model peptide similar in sequence to SpαI-1−156, to study their association affinities with a βI-spectrin peptide, SpβI-1898−2083, by isothermal titration calorimetry. We also determined their conformational flexibilities in solution by small-angle X-ray scattering (SAXS) methods. These two peptides exhibit sequence homology and could be expected to exhibit similar association affinities with β-spectrin. However, our studies show that the affinity of SpαII-1−149 with SpβI-1898−2083 is much higher than that of SpαI-1−156. Our SAXS findings also indicate a significantly more extended conformation for SpαII-1−149 than for SpαI-1−156. The radius of gyration values obtained by two different analyses of SAXS data and by molecular modeling all show a value of about 25 Å for SpαI-1−156 and of about 30 Å for SpαII-1−149, despite the fact that SpαI-1−156 has seven amino acid residues more than SpαII-1−149. For SpαI-1−156, the SAXS results are consistent with a flexible junction between helix C‘ and the triple helical bundle that allows multiple orientations between these two structural elements, in good agreement with our published NMR analysis. The SAXS findings for SpαII-1−149 support the hypothesis that this junction region is rigid (and probably helical) for αII brain spectrin. The nature of the junction region, from one extreme as a random coil (conformationally mobile) segment in αI to another extreme as a rigid segment in αII, determines the orientation of helix C‘ relative to the first structural domain. We suggest that this particular junction region in α-spectrin plays a major role in modulating its association affinity with β-spectrins, and thus regulates spectrin tetramer levels. We also note that these are the first conformational studies of brain spectrin." @default.
• W2020009604 created "2016-06-24" @default.
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• W2020009604 date "2003-11-18" @default.
• W2020009604 modified "2023-10-16" @default.
• W2020009604 title "Structural Analysis of the αN-Terminal Region of Erythroid and Nonerythroid Spectrins by Small-Angle X-ray Scattering" @default.
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• W2020009604 doi "https://doi.org/10.1021/bi0353833" @default.
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