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31.
Cutrona Carolyn E.; Cole Valerie; Colangelo Nicholas; Assouline Susan G.; Russell Daniel W. 《Canadian Metallurgical Quarterly》1994,66(4):687
Reports an error in "Perceived parental social support and academic achievement: An attachment theory perspective" by Carolyn E. Cutrona, Valerie Cole, Nicholas Colangelo, Susan G. Assouline and Daniel W. Russell (Journal of Personality and Social Psychology, 1994[Feb], Vol 66[2], 369-378). This article, which appeared in the Personality and Individual Differences section, was accepted for publication by Guest Editor Irwin Sarason. We wish to thank Professor Sarason for his help and to apologize for our oversight in not acknowledging this contribution. (The following abstract of the original article appeared in record 1994-31441-001.) Tested the extent to which parental social support predicted college GPA among undergraduates. A sample of 418 undergraduates completed the Social Provisions Scale--Parent Form (C. E. Cutrona; see record 1990-01422-001) and measures of family conflict and achievement orientation. American College Testing (ACT) Assessment Program college entrance exam scores (American College Testing Program, 1986) and GPA were obtained from the university registrar. Parental social support, especially reassurance of worth, predicted college GPA when controlling for academic aptitude (ACT scores), family achievement orientation, and family conflict. Support from parents, but not from friends or romantic partners, significantly predicted GPA. Results are interpreted in the context of adult attachment theory. (PsycINFO Database Record (c) 2010 APA, all rights reserved) 相似文献
32.
J Meyer J Gagnon J Gaillard M Lutz C Achim E Münck Y Pétillot CM Colangelo RA Scott 《Canadian Metallurgical Quarterly》1997,36(43):13374-13380
The rubredoxin from Clostridium pasteurianum contains a single iron atom bound to the polypeptide chain by cysteines 6, 9, 39, and 42. The C42A variant of this protein has been prepared by site-directed mutagenesis and heterologous expression of the gene in Escherichia coli. The mutated protein was found to contain an unexpected chromophore that has been characterized by a variety of techniques. UV-visible absorption and resonance Raman spectra were strongly reminiscent of those of [2Fe-2S] proteins. M?ssbauer spectra of the oxidized chromophore isolated in oxygen-free conditions indicated low-temperature diamagnetism resulting from antiferromagnetically coupled high-spin ferric ions. Analysis of X-ray absorption fine structure spectra yielded an Fe-Fe distance of 2.68 A. Colorimetric assays of iron and inorganic sulfide showed that the two elements are present in a 1:1 ratio. Electrospray-ionization mass spectra displayed a major component at M = 6190 Da, i.e. the molecular mass of the C42A apoprotein plus two atomic masses of iron and two atomic masses of sulfur. Taken together, these data show that a mere point mutation allows the stabilization of a binuclear [2Fe-2S] cluster in a protein that normally accommodates a mononuclear Fe(Scys)4 site. Assembly of a [2Fe-2S] cluster may occur because rubredoxin assumes a similar fold around its metal center as the [2Fe-2S] Rieske protein. Alternatively, a more extensive structural rearrangement of the polypeptide chain of the C42A rubredoxin variant may be considered as well. 相似文献