In instances where vegetation plays a dominant role in the riparian landscape, the type and characteristics of species, particularly a dominant invasive, can alter water velocity at high flows when vegetation is inundated. However, quantifying this resistance in terms of riparian vegetation has largely been ignored or listed as a secondary characteristic on roughness reference tables. We calculated vegetation roughness based on measurements of plant stem stiffness, plant frontal area, stem density, and stem area of three dominant herbaceous plants along the Sprague River, Oregon: the invasive reed canarygrass, native creeping spikerush, and native inflated sedge. Results show slightly lower roughness values than those predicted for vegetation using reference tables. In addition, native creeping spikerush and invasive reed canarygrass exhibit higher roughness values than native inflated sedge, which exhibits values lower than the other two species. These findings are of particular importance where the invasive reed canarygrass is outcompeting native inflated sedge, because with invasive colonization, roughness is increasing in channel zones and therefore is likely changing channel processes. Direct depositional measurements show similar results.

Extended retro (reversed) peptide sequences have not previously been accommodated within functional proteins. Here, we show that the entire transmembrane portion of the β-barrel of the pore-forming protein α-hemolysin can be formed by retrosequences comprising a total of 175 amino acid residues, 25 contributed by the central sequence of each subunit of the heptameric pore. The properties of wild-type and retro heptamers in planar bilayers are similar. The single-channel conductance of the retro pore is 15% less than that of the wild-type heptamer and its current-voltage relationship denotes close to ohmic behavior, while the wild-type pore is weakly rectifying. Both wild-type and retro pores are very weakly anion selective. These results and the examination of molecular models suggest that β-barrels may be especially accepting of retro sequences compared to other protein folds. Indeed, the ability to form a retro domain could be diagnostic of a β-barrel, explaining, for example, the activity of the retro forms of many membrane-permeabilizing peptides. By contrast with the wild-type subunits, monomeric retro subunits undergo premature assembly in the absence of membranes, most likely because the altered central sequence fails to interact with the remainder of the subunit, thereby initiating assembly. Despite this difficulty, a technique was devised for obtaining heteromeric pores containing both wild-type and retro subunits. Most probably as a consequence of unfavorable interstrand side-chain interactions, the heteromeric pores are less stable than either the wild-type or retro homoheptamers, as judged by the presence of subconductance states in single-channel recordings. Knowledge about the extraordinary plasticity of the transmembrane β-barrel of α-hemolysin will be very useful in the de novo design of functional membrane proteins based on the β-barrel motif.