Moving ideas: an exploration of students’ use of dialogue for writing in history

In this study, we explored how students make use of whole-class interaction in individual writing. Although various studies show the importance of classroom interaction for writing, little is known about how this works, particularly in history. Starting point is the idea that learning can move from the interpersonal level in classroom discourse to the intrapersonal level in subsequent individual writing. We analyzed nine student texts in history (Grade 11) and traced back the origins of the ideas used (documents or discussion). We found that students not only referenced both documents and classroom discussion in their texts but also that they developed additional ideas. We identified two ways in which students used classroom interaction in their texts: reproducing existing ideas or transforming existing ideas into new ones. Examples of both are discussed. Furthermore, we found differences in students’ use of the language of history in the discussion and in writing. When writing, students seemed to use more nominalizations and the language of time was more complex. We conclude that individual writing can benefit from whole-class discussion because students reproduced and transformed ideas in their writing, resulting in knowledge development, and because students’ use of the language of history became more proficient

A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1

<div><p>Crystallization of a maltose-binding protein MCL1 fusion has yielded a robust crystallography platform that generated the first apo MCL1 crystal structure, as well as five ligand-bound structures. The ability to obtain fragment-bound structures advances structure-based drug design efforts that, despite considerable effort, had previously been intractable by crystallography. In the ligand-independent crystal form we identify inhibitor binding modes not observed in earlier crystallographic systems. This MBP-MCL1 construct dramatically improves the structural understanding of well-validated MCL1 ligands, and will likely catalyze the structure-based optimization of high affinity MCL1 inhibitors.</p></div

The structure of Apo MBP-MCL1 determined at 1.90 Å.

<p>(A) The MBP domain (red) is connected by a short GS linker (orange) to MCL1 173–321 (blue). A portion of alpha helix four is not ordered in the structure (red dashed-line). Maltose ligand is shown in yellow. (B) The MCL1 domain is structurally very similar to the NMR structure of Apo-MCL1 (gray).</p

The structure of MBP-MCL1 bound to fragment 5 determined at 1.9 Å.

<p>Fragment <b>5</b> (yellow) binds similarly in comparison to the elaborated ligand from PDB ID 4OQ6 (gray).</p