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Office 365 ProPlus (2010)

The O365 ProPlus suite is a productivity suite for business users, containing a word processor (Word), spreadsheet (Excel), presentation (PowerPoint) and note taking (OneNote) application. In addition to this, it has a browser (Internet Explorer), document viewer (Office Online) and a calendar (Outlook). The most recent version of the suite (2013) included added support for search, integration with the Azure cloud (SharePoint, OneDrive), and a built-in FTP client. It also featured support for the OAuth 2.0 protocol, for OAuth providers such as Facebook, Google and Twitter.

For its compact nature, the suite has its own Windows Phone version of Outlook (Office Live Mail) and Windows 8.1 version of the Office 2013 desktop application. In addition to the 2013 version of Office, Microsoft offers Office 365 for its subscription service, which replaces the traditional license for the software with a subscription of Microsoft services. Office 365 is available to individuals or businesses.

In 2014, Microsoft announced that the 2013 version of Office 365 would be replaced with Office 2016. It includes the Word, Excel, PowerPoint and OneNote applications, as well as the Outlook mail client and OneDrive cloud storage services.


External links

Category:Microsoft Office
Category:Software using the GNU AGPL license
Category:Business softwareCharacterization of tertiary structure of human RNase H1.
RNase H1 is an essential component of RNA-dependent DNA polymerase for RNase H2-mediated RNA degradation. To understand the molecular mechanism of RNase H1 function, the tertiary structure of human RNase H1 has been characterized. Based on the crystal structure of Escherichia coli RNase HI, a structural model of human RNase H1 was constructed by homology modeling. Our structural model revealed that the Rnase H1 catalytic site is located at the N-terminal region of the protein, and the disordered C-terminal region could be folded into a conserved tetratricopeptide repeat domain. The conformation of conserved motifs was then constructed by molecular dynamics simulation. These results reveal the mechanism of catalysis of human RNase H1.People have been trying to turn a $539 million loss into a $1.2 billion profit for nearly two years — and their latest plan could put them in a position to do just


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