Mustguseal

Server for Multiple Structure-Guided Sequence Alignment of Protein Families

Mustguseal can automatically construct large structure based sequence alignments of protein families from all available information about their structures and sequences in public databases ...

... to study the diversity of protein mechanisms, annotate binding sites, identify and classify new family members.

A combination of structure and sequence alignment algorithms will be implemented to take into account complex structural and functional variability of proteins within a large superfamily

Version A 1.0; June 19th 2017



Want to get straight to the point with Mustguseal?
Step 1: Press the green button "Mustguseal it NOW!" above
Step 2: Scroll down, check out the "Algorithm outline" on the right side of the page
Step 3: Press the blue button "Demo mode"



The Mustguseal FAQs:


What is Mustguseal?
Mustguseal stands for Multiple Structure-Guided Sequence Alignment.
Mustguseal is a bioinformatic protocol - designed to build alignments of protein families and superfamilies, and a platform - a server to provide a user-friendly web-based interface to the Mustguseal protocol through the World Wide Web. Multiple alignments of thousands of protein sequences and structures can be automatically constructed using this public web-server. You should see the Presentation of the Mustguseal server for more information.


What does Mustguseal do?
Multiple alignments of thousands of protein sequences and structures can be automatically constructed using this public web-server. The Mustguseal protocol uses structure similarity search to collect remote evolutionary relatives, which are expected to represent different protein families. Then Mustguseal uses sequence similarity search to collect close evolutionary relatives - members of these families. In such a way Mustguseal takes into account complex structural and functional variability within a large superfamily to obtain a diverse set of homologous proteins. A combination of structure and sequence alignment procedures is then implemented to build the final multiple alignment.


What software is required to use Mustguseal?
All steps of the Mustguseal protocol are executed entirely on the server side. You do not need any specific software on your side.
The Analysis section of the Results page offers interactive content for sequence and structure analysis. Interactivity is implemented in HTML5 and therefore no plugins nor Java are required. The only prerequisite for viewing the Analysis section of the Results page is a HTML5-compatible web-browser. Current versions of all major browsers support HTML5 as the default standard.


What web-browser is required to use Mustguseal?
You do need a regular web-browser to use Mustguseal. To ensure the HTML5-compatibility upgrade your current browser to the latest version.
The server has been tested with the following browsers:

Please note that we have had compatibility issues with the Microsoft Internet Explorer and therefore this browser is currently not supported by the Mustguseal.


How to cite Mustguseal?
See this page for details.


How can a Mustguseal alignment help in your research?
You should use sister services of Mustguseal to further study the obtained alignments:

  • the Zebra web-service to identify variable amino acid residues responsible for functional diversity and to select hotspots for directed evolution or rational design experiments;
  • the pocketZebra web-service to identify and rank binding sites in proteins by functional significance and select particular positions in the structure that are important for selective binding of substrates/inhibitors/effectors;
  • the visualCMAT tool to study and interpret correlated mutations/co-evolving residues in protein structures.

Implementation of Mustguseal, Zebra, pocketZebra, and visualCMAT in the laboratory practice can help at studying mechanisms of protein action, designing enzymes with improved properties for practical application and selective modulators of activity of the wild-type proteins.

Suplatov, D., Kirilin, E., & Švedas, V. (2016). Bioinformatic Analysis of Protein Families to Select Function-Related Variable Positions. In Understanding Enzymes: Function, Design, Engineering, and Analysis (pp. 351-385) Ed. Allan Svendsen. Pan Stanford.

Suplatov, D., Voevodin, V., & Švedas, V. (2015). Robust enzyme design: Bioinformatic tools for improved protein stability. Biotechnology journal, 10(3), 344-355.

Suplatov, D., & Švedas, V. (2015). Study of functional and allosteric sites in protein superfamilies. Acta Naturae, 7(4), 27, 34-45.


Mustguseal support:

Dmitry Suplatov




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