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F. M. Goñi J. M. Valpuesta M. C. Barbero E. Rial J. I. G. Gurtubay J. M. Macarulla 《Cellular and molecular life sciences : CMLS》1984,40(2):193-195
Summary The solubilizing effect of Triton X-100 on beef heart submitochondrial particles (ETPH) has been studied under various physiological conditions. Coupled, uncoupled and azide-inhibited ETPH particles have been studied. Quantitative and qualitative differences are found in the proteins solubilized by the detergent from ETPH particles under the various conditions tested.Acknowledgments: This work was supported in part by a grant from a Spanish Comisión Asesora para la Investigación Cientifica y Técnica. M.C. Barbero was recipient of a scholarship from the Basque Government. 相似文献
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F M Go?i J M Valpuesta M C Barbero E Rial J I Gurtubay J M Macarulla 《Experientia》1984,40(2):193-195
The solubilizing effect of Triton X-100 on beef heart submitochondrial particles (ETPH) has been studied under various physiological conditions. Coupled, uncoupled and azide-inhibited ETPH particles have been studied. Quantitative and qualitative differences are found in the proteins solubilized by the detergent from ETPH particles under the various conditions tested. 相似文献
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Llorca O McCormack EA Hynes G Grantham J Cordell J Carrascosa JL Willison KR Fernandez JJ Valpuesta JM 《Nature》1999,402(6762):693-696
Chaperonins assist the folding of other proteins. Type II chaperonins, such as chaperonin containing TCP-1(CCT), are found in archaea and in the eukaryotic cytosol. They are hexadecameric or nonadecameric oligomers composed of one to eight different polypeptides. Whereas type I chaperonins like GroEL are promiscuous, assisting in the folding of many other proteins, only a small number of proteins, mainly actin and tubulin, have been described as natural substrates of CCT. This specificity may be related to the divergence of the eight CCT subunits. Here we have obtained a three-dimensional reconstruction of the complex between CCT and alpha-actin by cryo-electron microscopy and image processing. This shows that alpha-actin interacts with the apical domains of either of two CCT subunits. Immunolabelling of CCT-substrate complexes with antibodies against two specific CCT subunits showed that actin binds to CCT using two specific and distinct interactions: the small domain of actin binds to CCTdelta and the large domain to CCTbeta or CCTepsilon (both in position 1,4 with respect to delta). These results indicate that the binding of actin to CCT is both subunit-specific and geometry-dependent. Thus, the substrate recognition mechanism of eukaryotic CCT may differ from that of prokaryotic GroEL. 相似文献
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Ordering of a system of particles into its thermodynamically stable state usually proceeds by thermally activated mass transport of its constituents. Particularly at low temperature, the activation barrier often hinders equilibration--this is what prevents a glass from crystallizing and a pile of sand from flattening under gravity. But if the driving force for mass transport (that is, the excess energy of the system) is increased, the activation barrier can be overcome and structural changes are initiated. Here we report the reordering of radiation-damaged protein crystals under conditions where transport is initiated by stress rather than by thermal activation. After accumulating a certain density of radiation-induced defects during observation by transmission electron microscopy, the distorted crystal recrystallizes. The reordering is induced by stress caused by the defects at temperatures that are low enough to suppress diffusive mass transport. We propose that this defect-induced reordering might be a general phenomenon. 相似文献
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