This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. This project involves the structure determination of an octameric peptide that forms amyloid fibrils. Crystals with a long needle habit formed spontaneously from a D2O solution. We will determine the structure of the crystalline peptide using X-ray crystallography, utilizing a microfocus beamline in order to accommodate the extremely small size of the crystals (cross section approximately 3 x 3 micron). Because this peptide has a sequence that is significantly different from those of amyloid peptides of known structure, we anticipate that this structure will provide new information about the possible packing modes available to peptides and proteins in the fibrillar state.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR015301-07
Application #
7955154
Study Section
Special Emphasis Panel (ZRG1-BCMB-K (40))
Project Start
2009-04-01
Project End
2010-03-31
Budget Start
2009-04-01
Budget End
2010-03-31
Support Year
7
Fiscal Year
2009
Total Cost
$15,694
Indirect Cost
Name
Cornell University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
872612445
City
Ithaca
State
NY
Country
United States
Zip Code
14850
Chen, Wenyang; Mandali, Sridhar; Hancock, Stephen P et al. (2018) Multiple serine transposase dimers assemble the transposon-end synaptic complex during IS607-family transposition. Elife 7:
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