Publishing in education: A parallel session at the IUBMB/PSBMB 2019 "Harnessing Interdisciplinary Education in Biochemistry and Molecular Biology" conference.

Ensuring currency with trends, knowledge, and understanding of teaching and learning is essential for all educators. Researching learning and teaching is an enormous field which can range from examining the practical impact of new classes to research into the processes of learning. The "Publishing in Education" conference session discussed some of the approaches and outcomes of researching and publishing in education.

A History of Molecular Chaperone Structures in the Protein Data Bank.

Thirty years ago a class of proteins was found to prevent the aggregation of Rubisco. These proteins' ability to prevent unwanted associations led to their being called chaperones. These chaperone proteins also increased in expression as a response to heat shock, hence their label as heat shock proteins (Hsps). However, neither label encompasses the breadth of these proteins' functional capabilities. The term "unfoldases" has been proposed, as this basic function is shared by most members of this protein family. Onto this is added specializations that allow the different family members to perform various cellular functions. This current article focuses on the resolved structural bases for these functions. It reviews the currently available molecular structures in the Protein Data Bank for several classes of Hsps (Hsp60, Hsp70, Hsp90, and Hsp104). When possible, it discusses the complete structures for these proteins, and the types of molecular machines to which they have been assigned. The structures of domains and the associated functions are discussed in order to illustrate the rationale for the proposed unfoldase function.

The Hsp40 J-domain modulates Hsp70 conformation and ATPase activity with a semi-elliptical spring.

Regulatory protein interactions are commonly attributed to lock-and-key associations that bring interacting domains together. However, studies in some systems suggest that regulation is not achieved by binding interactions alone. We report our investigations on specific physical characteristics required of the Hsp40 J-domain to stimulate ATP hydrolysis in the Hsp40-Hsp70 molecular chaperone machine. Biophysical analysis using isothermal titration calorimetry, and nuclear magnetic resonance spectroscopy reveals the importance of helix rigidity for the maintenance of Hsp40 function. Our results suggest that the functional J-domain acts like a semi-elliptical spring, wherein the resistance to bending upon binding to the Hsp70 ATPase modulates the ATPase domain conformational change and promotes ATP hydrolysis.