Proteomics & Metabolomics
In addition to doing work on existing IGBB projects, the IGBB proteomics staff can
perform a variety of mass spectrometry and other proteomics services for MS State principal investigators and
IGBB collaborators. Such research can be performed through a Proposal Partnership,
a Research Agreement, or the Service Center.
The
IGBB's proteomics staff has considerable expertise in...
- Protein isolation/purification from all types of organisms/tissues
- 1D & 2D gel electrophoresis
- Gel- and non-gel-based mass spectrometry
- Protein identification
- Discovery and characterization of post-translational modifications;
- Quantitative proteomics
- Comparative proteomics & metabolomics
- Western blotting & protein visualization
- Integration of proteomic and nucleic acids data (e.g., proteogenomic
mapping)
- Functional annotation of proteins using Gene Ontology (GO)
standards and procedures
With regard to mass spectrometers, the IGBB's proteomics staff utilizes a ThermoFisher LTQ Orbitrap Velos, a Waters Nano ESI Q-TOF (model Xevo G2-S), and an Applied Biosystems (now ThermoFisher) MALDI TOF TOF. The LTQ Orbitrap Velos and the Nano ESI Q-TOF are fitted with upstream HPLC sample
purification systems.
To discuss the possibility of having the IGBB conduct
proteomics research in collaboration with you, please submit a ticket through the MyIGBB HelpDesk.
An IGBB proteomics consultant will respond to your query as quickly as possible
(usually within 24 hours).
A listing of IGBB Standard Services and their prices -- including information and prices for Training and Self-Service Equipment Usage -- is available in the Standard Services Catalog in MyIGBB and in PDF form via the link below.
ALSO SEE: Genomics (including Transcriptomics) | Biocomputing (Bioinformatics & Computational Biology)
NOTE: PIs are asked to consider whether the participation of an IGBB employee in a project merits that employee's inclusion as a co-author on a resulting manuscript(s). The decision ultimately lies with the PI. However, the IGBB encourages IGBB staff and faculty involved in
Proposal Partnerships and
Research Agreements to discuss/negotiate co-authorship with PIs before starting work on a project.
Mike NavickyDeputy Director of HPC
HPC ADMIN
email(662) 325-0779
Portera

Predictable convergence in hemoglobin function has unpredictable molecular underpinnings
IGBB Authors:
Federico G. HoffmannPUBLICATION YEAR:
2016IMPACT FACTOR:
19.87CITATION COUNT:
179Natarajan C, Hoffmann FG, Weber RE, Fago A, Witt CC, Storz JF (2016) Predictable convergence in hemoglobin function has unpredictable molecular underpinnings.
Science 354(6310): 336-339.
DOI:
10.1126/science.aaf9070EID:
2-s2.0-84992153922PMID: 27846568
DOWNLOAD PDFABSTRACTTo investigate the predictability of genetic adaptation, we examined the molecular basis of convergence in hemoglobin function in comparisons involving 56 avian taxa that have contrasting altitudinal range limits. Convergent increases in hemoglobin-oxygen affinity were pervasive among high-altitude taxa, but few such changes were attributable to parallel amino acid substitutions at key residues. Thus, predictable changes in biochemical phenotype do not have a predictable molecular basis. Experiments involving resurrected ancestral proteins revealed that historical substitutions have context-dependent effects, indicating that possible adaptive solutions are contingent on prior history. Mutations that produce an adaptive change in one species may represent precluded possibilities in other species because of differences in genetic background. © 2016, American Association for the Advancement of Science. All rights reserved.
The IGBB is supported, in part, by the following units:
The IGBB is an HPC² member center.