LINKS OF INTEREST
BACK
Cold
Spring Harbor Laboratories
-
________Berkeley Seminars
1)
Computational Biology - Wednesday at 4pm at 101 Life Sciences Addition
- http://computationalbiology.berkeley.edu/newsevents.asp
2) Structural Biology
- Mondays at 4pm at 100 Lewis - http://phobos.cchem.berkeley.edu/main/calendars/cf_editor/seminars/index.cfm?CFID=514284&CFTOKEN=7119f017855c1698-2BE78321-E0A9-263D-A0E6A883CC40E2CF
3) MCB -
Thursdays, 4pm at 100 Genetics and Plant Biology Building http://mcb.berkeley.edu/cgi-bin/seminars.cgi
4) Statistics
Thursdays 4pm at 1011 Evans - http://www.stat.berkeley.edu/users/sandrine/Teaching/PH292.S07/index.html
5) PMB -
Mondays 12 at 101 Barker - No
website yet, they are interviewing new faculty
6) Microbial
Biology- Wednesday 12 at 101
Barker hall - http://microbiology.berkeley.edu/mbss.htm
FIG: http://www.figresearch.com/
IMG: http://img.jgi.doe.gov/cgi-bin/pub/main.cgi
Microbes Online: http://www.microbesonline.org/
DISOPRED - http://bioinf.cs.ucl.ac.uk/disopred/
This server predicts natively disorder regions (encoded in the protein
sequence). These disordered regions represent flexible and dynamic regions.
Disorder regions can represent molecular recognition of proteins and nucleic
acids. ÒThe absence of a static structure means that disordered residues do not
appear in the electron density maps obtained by X-ray crystallography but they
can be investigated using other types of spectroscopy such as circular
dichroism and NMR (É)DISOPRED2 was trained on a set of around 750 non-redundant
sequences with high resolution X-ray structures. Disorder was identified with
those residues that appear in the sequence records but with coordinates missing
from the electron density map. This is an imperfect means for identifying
disordered residues as missing co-ordinates can also arise as an artifact of
the crystalization process. False assignment of order can also occur as a
result of stabilizing interactions by ligands or other macromolecules in the
complex. However, this is the simplest means for defining disorder in the
absence of further experimental investigation of the protein. A sequence
profile was generated for each protein using a PSI-BLAST search against a
filtered sequence database. The input vector for each residue was constructed
from the profiles of a symmetric window of fifteen positions. The data were
used to train linear support vector machines (SVMs). The SVM controls
overfitting by ensuring that the decision surface separates the two classes
with a large margin. An example linear decision surface that separates two classes
in 2DÓ – from the DISOPRED web-site.
Ward JJ, Sodhi
JS, McGuffin LJ, Buxton BF and Jones DT (2004)
Prediction and
functional analysis of native disorder in proteins from the three kingdoms of
life - Journal of Molecular Biology, 337, 635-645
Microarray
Database:
ONCOMINE: http://www.oncomine.org/resources/catalogModule/storeValue.jsp
Transmembrane
predictors:
THMM: http://www.cbs.dtu.dk/services/TMHMM/
Phobius: http://phobius.cgb.ki.se/
3-D structure
prediction:
PHYRE:
This is a new server that that recognizes a fold , the idea is that if there is
a protein with solved structure similar to your protein, they can try folding
it using the coordinates of the known structure (called threading, their
precedent is that the protein sequence folds by itself), this is worth giving
it a try. http://www.sbg.bio.ic.ac.uk/phyre/
3d-pssm:
This is the previous version of Phyre and is still my favorite http://www.sbg.bio.ic.ac.uk/~3dpssm/index2.html
JNET, a good secondary structure
predictor http://www.compbio.dundee.ac.uk/~www-jpred/jnet/
SCOP: http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.html
MODELLER: http://salilab.org/modeller/modeller.html
http://phylogenomics.berkeley.edu/cgi-bin/homology_model/build_model_data.py
Swiss model:
Predicting Domains:
PHYLOFACTS: Submit your protein to
phylofacts and see if there are domains already identified by this server
http://phylogenomics.berkeley.edu/phylofacts/input_phylofacts.php?library=structureprediction
SMART: http://smart.embl-heidelberg.de/
Superfamily: http://supfam.mrc-lmb.cam.ac.uk/SUPERFAMILY/
PFAM: Submit your protein to pfam
and see if there are domains already identified by this server
http://pfam.wustl.edu/hmmsearch.shtml
SCOP hierarchy, according to SCOP, protein domains in the
same SCOP superfamily are believed to be homologous.
Other remote homolog detection algorithms: Target98, Psi-Blast,
ISS, Fasta and Blast
Jake Glann GunvilleÕs handy toolkit
Germ Online - http://www.germonline.org/index.html
ÒThis gives information on the transcript, you can browse the
chromososmes, gene locus, É GermOnline is a cross-species knowledgebase that
provides classical and tiling microarray data relevant for the cell cycle and
gametogenesis. The report page integrates data on DNA sequence, RNA
concentration, length and exon composition as well as information on protein
function, structure and network interaction.Ó
Arabidopsis
Information Resource - http://www.arabidopsis.org/
ÒThe Arabidopsis Information Resource (TAIR) maintains a database
of genetic and molecular biology data for the model higher plant Arabidopsis thaliana.
Data available from TAIR includes the complete genome sequence along with gene
structure, gene product information,Ó
MIPS - http://mips.gsf.de/projects/plants
Database of
Interacting Proteins - http://dip.doe-mbi.ucla.edu/
ÒThe DIPTM database catalogs experimentally determined
interactions between proteins. It combines information from a variety of
sources to create a single, consistent set of protein-protein interactions. The
data stored within the DIP database were curated, both, manually by expert
curators and also automatically using computational approaches that utilize the
the knowledge about the protein-protein interaction networks extracted from the
most reliable, core subset of the DIP dataÓ
Entrez-Gene - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene
Flybase
- http://www.flybase.org/
Gene DB
- http://www.genedb.org/
Salmonella - http://www.salmonella.org/
EC – PDB THORTONÕS GROUP
EC DATABASE
Structure function
linkage Database
BPG WIKI
Genomes ONLINE
National Microbial Pathogen Data Resource
Risk Group Classification for
Infectious disease web-site
IntAct Site: IntAct provides a freely
available, open source database system and analysis tools for protein
interaction data. All interactions are derived from literature curation or
direct user submissions and are freely available.
HMM tutorial: http://www.soe.ucsc.edu/research/compbio/ismb99.tutorial.html
UCSC bioinformatics website
Sam tutorial
Dali. An
electronic mail/WWW server that performs a 3D similarity search in the PDB,
given the atomic coordinates of a 3D protein model as input (3). The analog of
a BLAST server for 3D structures. http://www2.embl-ebi.ac.uk/dali/
DSSP. A
database of secondary structure, solvent accessibility and other information
derived from 3D structures in the PDB. http://www.sander.embl-ebi.ac.uk/dssp/ ;
personal Email: sander@embl-ebi.ac.uk
GPCRDB.
Information system for G-protein coupled receptors. http://swift.embl-heidelberg.de/7tm/
; personal Email: vriend@embl-heidelberg.de
nrdb90. A
non-redundant sequence database that removes sequences at a redundancy level of
90% amino acid identity (15). Weekly updates.
http://www.embl-ebi.ac.uk/~holm/nrdb90
PredictProtein.
An electronic mail server that provides a predicted secondary structure and
solvent accessibility profile for any protein sequence with homologues in
Swiss-Prot. Rated at 72% sustained three-state accuracy (16).
http://www.embl-heidelberg.de/predictprotein/ ;
__________Process
of Go annotation
http://www.geneontology.org/GO.function.guidelines.shtml
amiGO
Open
Biomedical Ontologies is an umbrella web address for well-structured
controlled vocabularies for shared use across different biological and medical
domains.
Kegg: To downloads data click
here: ftp://ftp.genome.jp/pub/kegg/xml/
NCBI Bacterial genomes: ftp://ftp.ncbi.nih.gov/genbank/genomes/Bacteria/
All known genomes: Genomes online
COMPARATIVE GENOMES
http://genolist.pasteur.fr/Leproma/
Model Organism databases:
Model Organism Database/release
H. sapiens NCBI
36http://www.germonline.org/Homo_sapiens/index.html
M. musculus NCBI
m36http://www.germonline.org/Mus_musculus/index.html
R. norvegicus RGSC
3.4
D. rerio Zv
6
D. melanogaster BDGP 4
C. elegans WS
150
A. thaliana TIGR
S. pombe Sanger
S. cerevisiae SGD
1
UC-Extension
http://www.unex.berkeley.edu/cat/bio.html#drug