The enzyme portal integrates many resources, most of them hosted by EBI and also external ones such as BioPortal. Its main goal is to provide information about enzymes in a suitable format, with a usable interface designed for intended users. Instead of reinventing the wheel, it makes use of available and reliable resources to that end.

Related Literature:

http://nar.oxfordjournals.org/content/41/D1/D773.full

http://www.biomedcentral.com/1471-2105/14/103

Address of the bookmark: http://www.ebi.ac.uk/enzymeportal/

Requirements

You are (or soon will be) a master in bio-informatics. You have strong ICT skills and you are eager to fully submerge into the world of protein modeling. You have good experience with Linux and one or more programming languages as well as knowledge of tertiary structure analysis. Candidates with a Master degree in one of the life sciences (Biomedical sciences, Biochemistry, Bio-engineering, Biostatistics, …), with relevant interest and extended experience in this field are also welcome. A general background cancer biology and genetics is needed. You are willing and eligible to apply for a personal PhD fellowship with the Flemish FWO (FWO.be). Therefore, it is required that you hold a master degree from a European university, and have not obtained your master diploma more than three years ago (see FWO website for detailed conditions). Proficiency in English, and good communication skills, both oral and written, are required. You are highly motivated, and you like to work in an interactive research team. You are willing to work on a 4-year PhD project starting beginning of 2020.

What we offer

We offer a one year position, as a PhD student, which can be extended up to 4 year upon positive evaluation, even if a personal fellowship application is not successful. Wages are according to the standard Flemish bursary levels for PhD students.

Interested?
For additional information please contact dr. Geert Vandeweyer. To apply, send a copy of your CV including details of your relevant skills and a motivation letter by e-mail to dr. Geert Vandeweyer (geert.vandeweyer@uantwerpen.be) before March 15, 2020.

Source:https://academicpositions.be/ad/university-of-antwerp/2020/phd-student-bio-informatician-in-computational-protein-modeling/141252?utm_source=jooble&utm_medium=cpc&utm_campaign=jooble

More @ http://www.ncbs.res.in/sowdhamini/groups_sowdhamini.htm

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/