Evidence for three morphotypes among anadromous Arctic char (Salvelinus alpinus) sampled in the marine environment.

Variable resource use and responses to environmental conditions can lead to phenotypic diversity and distinct morphotypes within salmonids, including Arctic char (Salvelinus alpinus). Despite the cultural and economic importance of Arctic char in the Inuvialuit Settlement Region (ISR), limited data exist on the extent and presence of morphological diversity in this region. This is of concern for management given climate change impacts on regional fish populations.

A role for lakes in revealing the nature of animal movement using high dimensional telemetry systems.

Movement ecology is increasingly relying on experimental approaches and hypothesis testing to reveal how, when, where, why, and which animals move. Movement of megafauna is inherently interesting but many of the fundamental questions of movement ecology can be efficiently tested in study systems with high degrees of control. Lakes can be seen as microcosms for studying ecological processes and the use of high-resolution positioning systems to triangulate exact coordinates of fish, along with sensors that relay information about depth, temperature, acceleration, predation, and more, can be used to answer some of movement ecology's most pressing questions.

Shoal familiarity modulates effects of individual metabolism on vulnerability to capture by trawling.

Impacts of fisheries-induced evolution may extend beyond life history traits to more cryptic aspects of biology, such as behaviour and physiology. Understanding roles of physiological traits in determining individual susceptibility to capture in fishing gears and how these mechanisms change across contexts is essential to evaluate the capacity of commercial fisheries to elicit phenotypic change in exploited populations. Previous work has shown that metabolic traits related to anaerobic swimming may determine individual susceptibility to capture in trawls, with fish exhibiting higher anaerobic performance more likely to evade capture.

Folding pathway of an Ig domain is conserved on and off the ribosome.

Proteins that fold cotranslationally may do so in a restricted configurational space, due to the volume occupied by the ribosome. How does this environment, coupled with the close proximity of the ribosome, affect the folding pathway of a protein? Previous studies have shown that the cotranslational folding process for many proteins, including small, single domains, is directly affected by the ribosome. Here, we investigate the cotranslational folding of an all-β Ig domain, titin I27.