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Shim, Sang-Hee
Shim Research Lab
Research Interests
  • Super-resolution Optical Imaging
  • Single-molecule Biophysics
  • Ultrastructural Dynamics
  • Single-cell Systems Biology


Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR Spectroscopy

DC Field Value Language Strasfeld, David B. ko Ling, Yun L. ko Shim, Sang-Hee ko Zanni, Martin T. ko 2014-10-16T01:41:55Z - 2014-10-13 ko 2008-05 -
dc.identifier.citation JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.130, no.21, pp.6698 - + ko
dc.identifier.issn 0002-7863 ko
dc.identifier.uri -
dc.identifier.uri ko
dc.description.abstract Amyloid forming proteins have been implicated in many human diseases. The kinetics of amyloid fiber formation are of particular interest because evidence points to intermediate folding structures as potential cytotoxic species. The standard methods for monitoring the kinetics are to use fluorescence or circular dichroism spectroscopy, which do not uniquely resolve secondary structures. In this work, we use a new technology for rapidly scanning 2D-IR spectra that allows us to follow the fiber formation kinetics of the human islet amyloid polypeptide (hIAPP) that is involved in type II diabetes. Spectroscopic markers are identified that uniquely monitor random coil versus β-sheet secondary structures as well as probe β-sheet elongation and stacking. Our measurements provide more rigorous kinetics for the secondary structure evolution of amyloid formation than is available with other techniques. ko
dc.description.statementofresponsibility close -
dc.language ENG ko
dc.publisher AMER CHEMICAL SOC ko
dc.subject SIMULATION ko
dc.subject FIBRILS ko
dc.subject PEPTIDE ko
dc.title Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR Spectroscopy ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-44349183090 ko
dc.identifier.wosid 000256158200023 ko
dc.type.rims ART ko
dc.description.wostc 63 *
dc.description.scopustc 60 * 2015-05-06 * 2014-10-13 *
dc.identifier.doi 10.1021/ja801483n ko
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