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/

AutoDock

Stochastic (GA)

Flexible ligand and partially flexible target

ArgusLab

Systematic

Flexible ligandX-Score based

DOCK

Systematic (IC)

Flexible ligandDOCK 3.5 (force field)

eHITS

Systematic (RBD of fragments followed by reconstruction)Flexible ligand and partially flexible targetHiTS_Score (empirical)

FlexX

Systematic (IC)Flexible ligandFlexX SF (empirical)Commercial

FLIPDock

Stochastic (GA)Flexible ligand and flexible targetAUTODOCK (empirical)

FRED

Systematic (RBD)Flexible ligandChemScore, PLP, ScreenScore, ChemGauss (empirical/consensus)

GOLD

Stochastic (GA)

Flexible ligand and partially flexible targetGoldScore, ChemScore (empirical), ASP (knowledge based)

ICM

Stochastic (MC)

Flexible ligand and partially flexible targetICM SF (empirical)

ParDOCK

Stochastic (MC)

RigidBAPPL (empirical)

PLANTS

Stochastic (ACO)Flexible ligand and partially flexible target

CHEMPLP, PLP (empirical)

Surflex

Systematic (IC/MA)Flexible ligandHammerhead based (empirical)

Point to note:

Several studies have shown that the performance of most docking tools is highly dependent on the particular characteristics of both the binding site and the ligand to be investigated, and the determination which method would be more suitable in a specific context is difficult. We encouraged you to check several docking methods to determine which one(s) work best for your system.

Reads are simulated from both strands of a provided or randomly generated reference sequence.

Address of the bookmark: https://bitbucket.org/genomeinformatics/simlord/

Background/Motivation:

The dearth of structural information on alpha helical membrane protein (MPs) has hindered thus far the development of reliable knowledge –based potentials that can be used for automatic prediction of trans-membrane (TM) protein structure. While algorithm for identification of TM segments is available, modelling of the domains of alpha helical MPs involves assembling the segments into a bundle. This requires the correct assignment of the buried and lipid-exposed faces of the TM domains. 

Results: In a cross validated test on single sequences, our trans-membrane MM, correctly predicts the entire topology for 77% of the sequences in a standard dataset of 86 proteins with supervised topology. These results compare favorably with existing methods. 

Source Code: Matlab

Conclusion/Implementation: Here discriminant data mining approach was used to predict the location and orientation of alpha helices in membrane-spanning proteins. It is based on a first order Markov model (MM) with an architecture that corresponds closely to the biological systems. The model is enriched with three types of states for the loop on the cytoplasmic side (outer loop), loop for the non-cytoplasmic side (inner side), and trans-membrane part. The closed association between the biological and Markov states allows us to infer which part of the model architecture are important to capture the information which encodes the membrane topology, and gain a better understanding of the mechanism and constraints involved. Predictor Model was established by various  Markov decoder , and assignment of the membrane helix boundaries was apparent.

https://biosciences.hs-mittweida.de/equant/

Address of the bookmark: https://biosciences.hs-mittweida.de/equant/

Address of the bookmark: https://zhanglab.ccmb.med.umich.edu/STRUM/

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

Key Features of BLAST:
1. Sequence Comparison: BLAST searches for local alignments between the query sequence and sequences in a database. It identifies regions of similarity, which can help infer functional and evolutionary relationships.

2. Speed and Efficiency: BLAST uses heuristic algorithms, making it faster than exhaustive search methods, suitable for large-scale database searches.

3. Versatility: There are several versions of BLAST for different types of sequence comparisons:
- blastn: Compares a nucleotide query sequence against a nucleotide sequence database.
- blastp: Compares a protein query sequence against a protein sequence database.
- blastx: Compares a nucleotide query sequence translated in all reading frames against a protein sequence database.
- tblastn: Compares a protein query sequence against a nucleotide sequence database translated in all reading frames.
- tblastx: Compares the six-frame translations of a nucleotide query sequence against the six-frame translations of a nucleotide sequence database.

4. Scoring and E-value: BLAST results are scored based on the quality and length of the alignments. The E-value (expect value) indicates the number of alignments one can expect to find by chance, with lower E-values representing more significant matches.

5. Output Formats: BLAST provides results in various formats, including plain text, HTML, XML, and JSON, making it adaptable for different types of analyses and integrations with other tools.

Applications of BLAST:
- Genomic Research: Identifying genes, understanding genetic diversity, and mapping genome sequences.
- Protein Function Prediction: Inferring the function of unknown proteins by comparing them to known protein sequences.
- Evolutionary Studies: Exploring evolutionary relationships between organisms by comparing their genetic material.
- Medical Research: Identifying pathogens, understanding disease mechanisms, and developing treatments by comparing sequences of interest.

Overall, BLAST is an essential tool in bioinformatics, offering a reliable and efficient way to analyze and interpret biological sequence data.