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91.
92.
High-performance liquid chromatography provides direct evidence for substantial removal of naturally occurring specific free amino acids during a single passage of water through the mantle cavity of mussels. This occurs during the few seconds required for passage of the water across the gill, and removal proceeds unabated at ambient substrate concentrations as low as 38 nanomoles per liter. 相似文献
93.
Application of a comprehensive wave climate program to seven major deltas indicates that deltaic configurations and coastal landform combinations depend to a considerable degree on the wave power adjacent to the shore and on the river discharge relative to wave forces. Nearshore wave power is not correlative with deepwater wave power but, owing to frictional attenuation, is a function of the subaqueous slope. The subaqueous slope, in turn, depends partially on the slope and width of the continental shelf but primarily on the rate at which the river can supply sediments to the nearshore zone. River-dominated configurations result only when the river is able to build flat offshore profiles, which reduce nearshore wave power; where the subaqueous slope is steep, waves reach the shore comparatively undiminished and wave-built forms prevail. 相似文献
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Uhlmann WR Bennett R Botkin JR Botstein D Boughman JA Chakravarti A Clayton EW Kahn J Koenig B Murray TH Olson MV Rowley J Terry S Valle D 《Science (New York, N.Y.)》2003,299(5612):1515; author reply 1515
96.
Wright GD 《Science (New York, N.Y.)》2007,315(5817):1373-1374
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99.
Bartke A Wright JC Mattison JA Ingram DK Miller RA Roth GS 《Science (New York, N.Y.)》2002,296(5576):2141-2; author reply 2141-2
100.
Structural characterization of a partly folded apomyoglobin intermediate 总被引:41,自引:0,他引:41
To understand why proteins adopt particular three-dimensional structures, it is important to elucidate the hierarchy of interactions that stabilize the native state. Proteins in partly folded states can be used to dissect protein organizational hierarchies. A partly folded apomyoglobin intermediate has now been characterized structurally by trapping slowly exchanging peptide NH protons and analyzing them by two-dimensional 1H-NMR (nuclear magnetic resonance). Protons in the A, G, and H helix regions are protected from exchange, while protons in the B and E helix regions exchange freely. On the basis of these results and the three-dimensional structure of native myoglobin, a structural model is presented for the partly folded intermediate in which a compact subdomain retains structure while the remainder of the protein is essentially unfolded. 相似文献