57 research outputs found
Becoming us and them : Social learning and intergroup bias
In recent years, research has demonstrated that the basic features of prejudice and discrimination emerge early in children’s development. These discoveries call into question the role of social learning in intergroup bias. Specifically, through what means do we learn to distinguish “us” from “them”? Here we explore this question, focusing on three key issues: how children respond to biased information they receive from others, how children selectively seek out certain types of biased information, and how children communicate biased information to others. We close by discussing the implications of this research for interventions to reduce stereotyping, prejudice and discrimination
A pawn in someone else's game?: The cognitive, motivational, and paradigmatic barriers to women's excelling in negotiation
Women's relatively worse performance in negotiation is often cited as an explanation for gender differences in advancement and pay within organizations. We review key findings from the past twenty years of research on gender differences in negotiation. Women do underperform relative to men in negotiation, but only under limited circumstances, which means the performance gap is unlikely due to lesser skills on their part. The barriers between women and negotiation excellence are of three types: cognitive, motivational, and paradigmatic. Cognitive barriers stem from negative stereotypes about women's negotiating abilities. Motivational barriers stem from desire to prevent women negotiators from excelling in a masculine domain. Paradigmatic barriers stem from how negotiation is currently studied. We call for greater attention to motivational barriers and for changes to the negotiation paradigm. Women negotiators are not incompetent, and training them to negotiate more like men is not obviously the solution. In fact, women have greater concern for others than men do, and their cooperativeness elevates collective intelligence and enables ethical behavior. Under a new paradigm of negotiation, the value of these strengths could become more readily apparent. In particular, we advocate for greater attention to long-term relationships, subjective value, and relational capital, all of which may have important economic implications in real world negotiations
Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
The fact that natural β-sheet proteins are usually soluble but that fragments or designs of β structure usually aggregate suggests that natural β proteins must somehow be designed to avoid this problem. Regular β-sheet edges are dangerous, because they are already in the right conformation to interact with any other β strand they encounter. We surveyed edge strands in a large sample of all-β proteins to tabulate features that could protect against further β-sheet interactions. β-barrels, of course, avoid edges altogether by continuous H-bonding around the barrel cylinder. Parallel β-helix proteins protect their β-sheet ends by covering them with loops of other structure. β-propeller and single-sheet proteins use a combination of β-bulges, prolines, strategically placed charges, very short edge strands, and loop coverage. β-sandwich proteins favor placing an inward-pointing charged side chain on one of the edge strands where it would be buried by dimerization; they also use bulges, prolines, and other mechanisms. One recent β-hairpin design has a constrained twist too great for accommodation into a larger β-sheet, whereas some β-sheet edges are protected by the bend and reverse twist produced by an Lβ glycine. All free edge strands were seen to be protected, usually by several redundant mechanisms. In contrast, edge strands that natively form β H-bonded dimers or rings have long, regular stretches without such protection. These results are relevant to understanding how proteins may assemble into β-sheet amyloid fibers, and they are especially applicable to the de novo design of β structure. Many edge-protection strategies used by natural proteins are beyond our current abilities to constrain by design, but one possibility stands out as especially useful: a single charged side chain near the middle of what would ordinarily be the hydrophobic side of the edge β strand. This minimal negative-design strategy changes only one residue, requires no backbone distortion, and is easy to design. The accompanying paper [Wang, W. & Hecht, M. H. (2002) Proc. Natl. Acad. Sci. USA 99, 2760–2765] makes use of the inward-pointing charge strategy with great success, turning highly aggregated β-sandwich designs into soluble monomers
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