OSU Navigation Bar

The Ohio State University University Libraries Knowledge Bank

CW THZ SPECTROSCOPY OF SMALL PEPTIDES

Please use this identifier to cite or link to this item: http://hdl.handle.net/1811/30569

Show full item record

Files Size Format View
abstract.gif 19.95Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES
OSU_siegrist.ppt 13.46Mb Microsoft PowerPoint View/Open
AVI_AAAap8_2_Mercury.avi 678Kb Unknown View/Open
AVI_AAA10_Tinker4.avi 2.214Mb Unknown View/Open
AP_HBONDS.avi 3.025Mb Unknown View/Open
AAA2_AB_III_631_B3_v1.avi 1.792Mb Unknown View/Open
AAA2_AB_III_631_B3_v191.avi 1.344Mb Unknown View/Open
Slide1.GIF 58.47Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES
Slide2.GIF 18.35Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES
Slide3.GIF 52.15Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES
Slide4.GIF 72.36Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES
Slide5.GIF 61.73Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES
Slide6.GIF 17.51Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES
Slide7.GIF 49.62Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES
Slide8.GIF 78.46Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES
Slide9.GIF 53.99Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES
Slide10.GIF 68.12Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES
Slide11.GIF 56.05Kb GIF image Thumbnail of CW THZ SPECTROSCOPY OF SMALL PEPTIDES

Title: CW THZ SPECTROSCOPY OF SMALL PEPTIDES
Creators: Siegrist, K.; Plusquellic, D. F.; Balu, R.; Gregurick, S.; Mandelbaum, I.; Walker, A. R. Hight
Issue Date: 2005
Abstract: CW THz spectroscopy has been used to investigate the lowest frequency vibrational modes of small peptides. Due to their non-local character, these large amplitude modes are remarkably sensitive to intermolecular hydrogen bonding. THz spectra obtained from 2 \wn to 100 \wn, for three different crystalline forms of alanine tripeptide at 4.2 K were all quite different. These three forms included one parallel and two anti-parallel beta sheet structures. The latter two forms differ only in the presence and absence of water molecules that bridge and cross link the sheets. Despite the weak nature of the water hydrogen bonds, the THz spectra for the hydrated and dehydrated antiparallel structures of trialanine are drastically different, while spectra observed for the two forms in the mid-infrared region were indistinguishable. Together with data obtained at intermediate hydration levels, these results provide insight into the nature and scope of forces fields necessary to model these low energy interactions. Spectral predictions obtained for crystal-like structures using the CHARMM force field and for various dimer forms from density functional theory will be discussed.
URI: http://hdl.handle.net/1811/30569
Other Identifiers: 2005-TF-02
Bookmark and Share