Climate windows for Polynesian voyaging to New Zealand and Easter Island.

Debate about initial human migration across the immense area of East Polynesia has focused upon seafaring technology, both of navigation and canoe capabilities, while temporal variation in sailing conditions, notably through climate change, has received less attention. One model of Polynesian voyaging observes that as tradewind easterlies are currently dominant in the central Pacific, prehistoric colonization canoes voyaging eastward to and through central East Polynesia (CEP: Society, Tuamotu, Marquesas, Gambier, Southern Cook, and Austral Islands) and to Easter Island probably had a windward capacity. Similar arguments have been applied to voyaging from CEP to New Zealand against prevailing westerlies. An alternative view is that migration required reliable off-wind sailing routes. We investigate the marine climate and potential voyaging routes during the Medieval Climate Anomaly (MCA), A.D. 800-1300, when the initial colonization of CEP and New Zealand occurred. Paleoclimate data assimilation is used to reconstruct Pacific sea level pressure and wind field patterns at bidecadal resolution during the MCA. We argue here that changing wind field patterns associated with the MCA provided conditions in which voyaging to and from the most isolated East Polynesian islands, New Zealand, and Easter Island was readily possible by off-wind sailing. The intensification and poleward expansion of the Pacific subtropical anticyclone culminating in A.D. 1140-1260 opened an anomalous climate window for off-wind sailing routes to New Zealand from the Southern Austral Islands, the Southern Cook Islands, and Tonga/Fiji Islands.

The folding of a family of three-helix bundle proteins: spectrin R15 has a robust folding nucleus, unlike its homologous neighbours.

Three homologous spectrin domains have remarkably different folding characteristics. We have previously shown that the slow-folding R16 and R17 spectrin domains can be altered to resemble the fast folding R15, in terms of speed of folding (and unfolding), landscape roughness and folding mechanism, simply by substituting five residues in the core. Here we show that, by contrast, R15 cannot be engineered to resemble R16 and R17. It is possible to engineer a slow-folding version of R15, but our analysis shows that this protein neither has a rougher energy landscape nor does change its folding mechanism. Quite remarkably, R15 appears to be a rare example of a protein with a folding nucleus that does not change in position or in size when its folding nucleus is disrupted. Thus, while two members of this protein family are remarkably plastic, the third has apparently a restricted folding landscape.

Separating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains.

The elongated three-helix bundle domains spectrin R16 and R17 fold some two to three orders of magnitude more slowly than their homologue R15. We have shown that this slow folding is due, at least in part, to roughness in the free-energy landscape of R16 and R17. We have proposed that this roughness is due to a frustrated search for the correct docking of partly preformed helices. However, this accounts for only a small part of the slowing of folding and unfolding. Five residues on the A helix of R15, when inserted together into R16 or R17, increase the folding rate constants, reduce landscape roughness, and alter the folding mechanism to one resembling R15. The effect of each of these mutations individually is investigated here. No one mutation causes the behavior seen for the five in combination. However, two mutations, E18F and K25V, significantly increase the folding and unfolding rates of both R16 and R17 but without a concomitant loss in landscape roughness. E18F has the greatest effect on the kinetics, and a Φ-value analysis of the C helix reveals that the folding mechanism is unchanged. For both E18F and K25V the removal of the charge and resultant transition state stabilization is the main origin of the faster folding. Consequently, the major cause of the unusually slow folding of R16 and R17 is the non-native burial of the two charged residues in the transition state. The slowing due to landscape roughness is only about fivefold.