This resource is a video abstract of a research paper created by Research Square on behalf of its authors. It provides a synopsis that's easy to understand, and can be used to introduce the topics it covers to students, researchers, and the general public. The video's transcript is also provided in full, with a portion provided below for preview:

"The bacterial flagellum is one of the most amazing structures in biology. The whip-like appendage rotates as many as 300 times per second, allowing bacteria to swim around. That speed is thanks to a powerful internal motor, and a strong hook that acts as a universal joint and transmits torque. Scientists know a lot about how these machines work, but there are still important questions, like how hook proteins function. Now, researchers at the Okinawa Institute of Science and Technology and their collaborators have identified a surprisingly important role for a disordered segment of the hook protein. The biologists first noticed that many bacterial species share a 40- to 60-residue section of their rod and hook proteins. This part lacks structure and is considered intrinsically disordered, but it might, in its flexibility, be essential. The team named this peptide ID-Rod-Stretch since it was conserved in length in the rod protein, but varied in the hook protein..."

The rest of the transcript, along with a link to the research itself, is available on the resource itself.

This resource is a video abstract of a research paper created by Research Square on behalf of its authors. It provides a synopsis that's easy to understand, and can be used to introduce the topics it covers to students, researchers, and the general public. The video's transcript is also provided in full, with a portion provided below for preview:

"Class 1 cytokine receptors, or C1CRs, are transmembrane proteins that facilitate communication between the inside and outside of cells. They orchestrate key processes such as proliferation, differentiation, immunity, and growth largely through long intracellular domains (ICDs) – forming C1CR-ICDs. A recent study shows that C1CR-ICDs share being fully disordered and brimming with short linear motifs, or SLiMs, which are compact amino acid sequences that mediate protein interactions. How can disorder govern this critical signaling capacity? Many of these SLiMs are overlapping, indicating a complex regulation of interactions. Together with a different amino composition compared to other IDPs, this enables the C1CR-ICDs to execute distinct functions. Thus, organizational and functional features are embedded within the disorder of the C1CR-ICDs but remain to be decoded..."

The rest of the transcript, along with a link to the research itself, is available on the resource itself.

This site takes us into the world of structural biology -- a branch of molecular biology that focuses on the shape of nucleic acids and proteins (the molecules that do most of the work in our bodies). Learn about the structures and roles of proteins, tools used to study protein shapes, how proteins are used in designing new medications (for AIDS and arthritis), and what structural biology reveals about all life processes. Find out about careers in biomedical research.