Address of the bookmark: http://kobas.cbi.pku.edu.cn/

Caretta, a multiple structure alignment suite meant for homologous but sequentially divergent protein families which consistently returns accurate alignments with a higher coverage than current state-of-the-art tools. Caretta is available as a GUI and command-line application and additionally outputs an aligned structure feature matrix for a given set of input structures, which can readily be used in downstream steps for supervised or unsupervised machine learning. 

Address of the bookmark: http://www.bioinformatics.nl/caretta/

Now my main interests are in gene regulation, where we work on promoter analysis; non-coding RNA, where miRNAs and structure prediction are the main areas; and protein structure, where the group is working on methods for structure prediction from sequence. To read more about these topics, please see the research pages.

Lab page @ http://wiki.binf.ku.dk/User:Krogh

the study of the sequence-structure relationship
(application -> structure prediction)
the study of the structure-function relationship
(application -> function prediction)

Therefore, anything related to the configuration (sequence) and conformation (structure) in atomic systems of proteins and nucleic acids, and the interaction of these with other elements (function) is of our major interest.

Lab page @ http://melolab.org/mbl/

Now, two research groups have engineered new optogenetic proteins that can be used to efficiently silence neurons. One of the two new proteins comes from the lab of Karl Deisseroth, a psychiatrist and neuroscientist at Stanford University who helped develop optogenetics as a research tool. His group’s new “off” switch for neurons was created by changing 10 of the 333 amino acids in an existing optogenetic protein, which itself had been engineered by combining natural proteins from green algae. That advance “creates a powerful tool that allows neuroscientists to apply a brake in any specific circuit with millisecond precision,” said Thomas Insel, director of the National Institute of Mental Health, in a released statement. The other new silencing protein, developed by scientists at the Humboldt University of Berlin and collaborators, was created by changing amino acids in the same existing optogenetic protein. 

Some researchers are also looking to optogenetics as a potential treatment for patients with a variety of conditions (see “For Mice, and Maybe Men, Pain Is Gone in a Flash,” and “Flipping on the Lights to Halt Seizures”) but there are huge challenges to overcome. The method requires genetic modification of cells to make them light-sensitive. It also requires implanted light sources for all but the shallowest of nerve endings.

Summary: The application of protein–protein docking in large-scale interactome analysis is a major challenge in structural bioinformatics and requires huge computing resources. In this work, we present MEGADOCK 4.0, an FFT-based docking software that makes extensive use of recent heterogeneous supercomputers and shows powerful, scalable performance of over 97% strong scaling.

Availability and Implementation: MEGADOCK 4.0 is written in C++ with OpenMPI and NVIDIA CUDA 5.0 (or later) and is freely available to all academic and non-profit users at: http://www.bi.cs.titech.ac.jp/megadock.

Contact: akiyama@cs.titech.ac.jp

Address of the bookmark: http://bioinformatics.oxfordjournals.org/content/early/2014/08/06/bioinformatics.btu532.short

MutaBind guides you through this process, step by step, starting with selecting a protein complex and inputting PDB code or uploading PDB files. You can also retrieve results with a job ID number, view help documents, and review the MutaBind method and references.

More at http://www.ncbi.nlm.nih.gov/projects/mutabind/index.fcgi/

Address of the bookmark: http://www.compbio.dundee.ac.uk/jpred4/