BOL: Related items

PSPairwise Sequentially Markovian Coalescent (PSMC) model

Jit — Thu, 19 Apr 2018 05:29:23 -0500

Implementation of the Pairwise Sequentially Markovian Coalescent (PSMC) model

Address of the bookmark: https://github.com/lh3/psmc

Master Thesis: Trans-membrane topology prediction through Markov based decoders

Rahul Agarwal — Wed, 17 Jul 2013 16:16:17 -0500

Abstract:

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.

eQuant : energy-based quality assessment of protein

Shruti Paniwala — Sat, 24 Jun 2017 19:24:24 -0500

Protein structures are of varying quality. Especially, in-silico modeled structures are prone to contain serious errors, which limit the usefulness and reliability of these particular protein structures.

eQuant is a service for structure quality assessment of single proteins, which utilizes a coarse-grained energy model. The overall quality is calculated as well as the reliability of individual residues. You can submit single PDB files or archives containing a set of proteins.

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

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

STRUM: structure-based prediction of protein stability changes upon single-point mutation

BioStar — Mon, 10 Sep 2018 13:21:49 -0500

STRUM is a method for predicting the fold stability change (ΔΔG) of protein molecules upon single-point nsSNP mutations. STRUM adopts a gradient boosting regression approch to train the Gibbs free-energy changes on a variety of features at different levels of sequence and structure properties. The unique characteristics of STRUM is the combination of sequence profiles with low-resolution structure models from protein structure prediction, which helps enhance the robustness and accuracy of the method and make it applicable to various protein seqences, including those without experimental structures

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

PhD student / Bio-informatician in computational protein modeling

Sun, 23 Feb 2020 03:46:46 -0600

PhD student / Bio-informatician in computational protein modeling
Job Profile
You will perform research on drug/protein interaction analysis in the context of lung cancer, using computational protein modeling. You will implement existing models predicting drug efficacy, related to EGFR-driven cancer. You will translate these models to novel oncogenes, including ROS1. You will validate these models against experimental data from a parallel project, with the final goal of deployment of your methods into clinical decision making. Your work will be embedded in an international network consisting of both academic partners and ROS1-NSCLC patient organizations.

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

Basics of BLAST Programs !

BioStar — Fri, 26 Jul 2024 06:04:26 -0500

The Basic Local Alignment Search Tool (BLAST) is a powerful bioinformatics program used to compare an input sequence (such as DNA, RNA, or protein sequences) against a database of sequences to find regions of similarity. Developed by the National Center for Biotechnology Information (NCBI), BLAST is widely used for identifying species, finding functional and evolutionary relationships between sequences, and predicting the function of novel sequences.

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.

An entire genome written in lab

Rahul Nayak — Fri, 25 Oct 2013 09:43:03 -0500

This is the first time ever the genetic code has been fundamentally changed. The breakthrough is a huge step forward in synthetic biology and opens up the possibility of turning re-coded bacteria into biofactories, capable of producing potent new forms of protein that could fight disease or generate sustainable materials.

More @ http://news.yale.edu/2013/10/17/researchers-rewrite-entire-genome-and-add-healthy-twist

News Reference: Yale news

Image Source: Sciencedaily.

GABi

Fri, 06 Dec 2013 16:43:01 -0600

GABi Research
The major researching fields defined as the GABi scope are described next:
Sequence Analysis
Protein Structure Prediction
Comparative Genomics
Functional Analysis of Residues on Protein Families
Gene/Protein Networks
Genome structure & base composition
Highthroughput data analysis from NGS

Lab Page http://gabi.cidbio.org/index/

Scientists map 17,294 proteins produced in human body

Jit — Thu, 29 May 2014 01:57:55 -0500

Indian scientists missed the genomic profiling bus, but they've more than made up for it by creating the first human proteome map which is an extension of the genomic study. Till now, here is no direct equivalent for the human proteome. But recently two groups present mass spectrometry-based analysis of human tissues, body fluids and cells mapping the large majority of the human proteome.

The Indian scientists working in Bangalore, along with their American counterparts, have mapped more than 17,000 proteins in 30 organs of the human body. Just like the human genome was sequenced around the turn of the millennium, this is an equivalent mapping of the human proteome.

The researcher estimated there are around 20,500 proteins in the human body. These scientists have profiled around 17,294, which account for around 84% of the total proteins. Apart from this, the team also traced around 2,500 of 3,000 proteins that had been categorised as "missing proteins".

The work, done by group of Indian scientists, and Johns Hopkins University, published in the renowned journal Nature ( http://www.nature.com/nature/journal/v509/n7502/full/nature13302.html ). Of the 72 people who worked on the project, 46 are Indians.

Reference:

http://www.nature.com/nature/journal/v509/n7502/full/nature13302.html

http://www.proteinatlas.org/ -The antibody-based Human Protein Atlas programme

http://www.humanproteomemap.org/ -Proteogenomic analysis by identifying translated proteins from annotated pseudogenes, non-coding RNAs and untranslated regions.

https://www.proteomicsdb.org/ -Assembled protein evidence for 18,097 genes in ProteomicsDB

Amino Acid Flash Tutorial

Jit — Mon, 11 Aug 2014 08:58:17 -0500

Protein is a part of every cell in your body, and no other nutrient plays as many different roles in keeping you alive and healthy. Protein is the building block of our body, and amino acids are the main areas of interest. We have emphasized on all 20 amino acids in this documentary movie. This documentary has been developed that emphasize on chemical structure, chemical formula, IUPAC name and other detail information of all 20 amino acids with the voice, picture with interactive button. This will be helpful for the entire biology and bioinformatics student.

How to run?

You need to install flash player or open it with web browser ( I guess you have installed flash plugin) to play.

Comment below if you like it. Thanks