A new method for collecting 2D-IR spectra that utilizes both a pump-probe beam geometry and a mid-IR pulse shaper is used to gain a fuller understanding of fiber formation in the human islet amyloid polypeptide (hIAPP). We extract structural kinetics in order to better understand aggregation in hIAPP, the protein component of the amyloid fibers found to inhibit insulin production in type II diabetes patients.
|Title of host publication||Springer Series in Chemical Physics|
|Publisher||Springer Science and Business Media Deutschland GmbH|
|Number of pages||3|
|Publication status||Published - 2009|
|Name||Springer Series in Chemical Physics|
Bibliographical noteFunding Information:
We acknowledge the contributions of Dan Raleigh and Peter Marek from SUNY – Stony Brook for synthesizing the isotope labeled hIAPP. Funding comes from the NSF (CHE-0350518), the Packard Foundation, and the NIH (R21AI064797, R01DK079895).
© 2009, Springer-Verlag Berlin Heidelberg.
- Amyloid Fiber
- Amyloid Formation
- Cross Peak
- Fiber Formation
- Random Coil
ASJC Scopus subject areas
- Physical and Theoretical Chemistry