Protein structure gets exciting

Examination of Protein Complexes Gets SiMPull.

Spectra of some self - exciting and mutually exciting point processes

In recent years methods of data analysis for point processes have received some attention, for example, by Cox & Lewis (1966) and Lewis (1964). In particular Bartlett (1963a, b) has introduced methods of analysis based on the point spectrum. Theoretical models are relatively sparse. In this paper the theoretical properties of a class of processes with particular reference to the point spectrum ...

Revealing what gets buried first in protein folding.

After decades of research, the nature of the rate-limiting step in the folding of globular proteins still elicits a range of opinions (1). The properties of the associated transition state (TS) provide critical insights into possible folding mechanisms. However, the characterization of the TS is challenging because atomic level methods cannot be applied to this minimally populated state, and lo...

Protein stability: The COP9 signalosome gets in on the act

The COP9 signalosome is a multiprotein complex somewhat similar to the lid component of the 26S proteasome. Recent studies suggest that it regulates the stability of proteins by interfering with the ubiquitin-proteasome pathway via deneddylation and phosphorylation.

Exciting rogue waves

Rogue waves [1]—extreme ocean waves with heights up to thirty meters—have been common elements in stories from people working at sea, as well as in popular fiction. It is not hard to imagine why: being on a small boat in a stormy sea swell and suddenly encountering a wave maybe three times as high as the surrounding waves is a terrifying experience (Fig. 1). However, up to a few decades ago, oc...