{"id":26,"date":"2017-03-08T14:49:15","date_gmt":"2017-03-08T19:49:15","guid":{"rendered":"https:\/\/my.dev.vanderbilt.edu\/buchanan\/?page_id=26"},"modified":"2023-03-27T14:50:21","modified_gmt":"2023-03-27T19:50:21","slug":"publications","status":"publish","type":"page","link":"https:\/\/my.dev.vanderbilt.edu\/buchanan\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"<p><span style=\"text-decoration: underline\"><em>Publications while at Vanderbilt University<\/em><\/span><\/p>\n<p>19.\u00a0Kelsey Rochelle Webb, Kayla Anne Hess, Alisa Shmidt, Kathryn Diane Segner, Lauren Elizabeth Buchanan,\u00a0Probing local changes to \u03b1-helical structures with 2D IR spectroscopy and isotope labeling,\u00a0Biophysical Journal (2023), doi:\u00a0https:\/\/doi.org\/10.1016\/j.bpj.2023.03.014.<\/p>\n<p>18.\u00a0<span class=\"contrib-author\">Kayla A. Hess<i class=\"pubContent-comma\">, <\/i><\/span><span class=\"contrib-author\">Nathan J. Spear<i class=\"pubContent-comma\">, <\/i><\/span><span class=\"contrib-author\">Sophia A. Vogelsang<i class=\"pubContent-comma\">, <\/i><\/span><span class=\"contrib-author\">Janet E. Macdonald<i class=\"pubContent-comma\">, and <\/i><\/span><span class=\"contrib-author\">Lauren E. Buchanan <\/span><span class=\"citation_info\"><span class=\"articleName\">, &#8220;Determining the impact of gold nanoparticles on amyloid aggregation with 2D IR spectroscopy&#8221;<\/span><span class=\"journalName\">, J. Chem. Phys.<\/span> <span class=\"volume\">158<\/span>, 091101 <span class=\"year\">(2023)<\/span> https:\/\/doi.org\/10.1063\/5.0136376<\/span><\/p>\n<p>17. W.B. Weeks, L.E. Buchanan. \u201cLabel-free detection of \u03b2-sheet polymorphism,\u201d\u00a0<em>Journal of Physical Chemistry Letters, <\/em>13, 9534-9538 (2022). https:\/\/doi.org\/10.1021\/acs.jpclett.2c02292<\/p>\n<p>16.\u00a0R.E. Wilkinson, K.N. Kraichely, C.M. Hendy, L.E. Buchanan, S. Parnham, M.W. Giuliano. \u201cThe neuropeptide galanin adopts an irregular secondary structure,\u201d <em>Biochemical and Biophysical Research Communications<\/em>, 626, 121-128 (2022).\u00a0DOI:\u00a0<a href=\"http:\/\/doi.org\/10.1016\/j.bbrc.2022.08.032\" target=\"_blank\">10.1016\/j.bbrc.2022.08.032<\/a><\/p>\n<p>15. Weeks WB, Tainter CJ, Buchanan LE, Investigating the effects of N-terminal acetylation on KFE8 self-assembly with 2D IR spectroscopy, Biophysical Journal (2022), doi: https:\/\/ doi.org\/10.1016\/j.bpj.2022.03.003.<\/p>\n<p>14. L.E. Buchanan, W. Xiong. \u201cTwo-dimensional Infrared (2D IR) Spectroscopy.\u201d In: R. Guenther and D. Steel, ed.,\u00a0<em>Encyclopedia of Modern Optics II, 2nd ed.<\/em> Oxford: Elsevier, pp 164-183.<\/p>\n<p><span style=\"text-decoration: underline\"><em>Publications prior to Vanderbilt Universi<\/em><em>ty<\/em><\/span><\/p>\n<p>13. L.E. Buchanan, M. Maj, E.B. Dunkelberger, P.-N. Cheng, J.S. Nowick, M.T. Zanni. \u201cAmyloid polymorphs reveal competing pathways for the formation of hIAPP fibrils and help identify the transition state,\u201d <em>Journal of the American Chemical Society<\/em>, submitted Mar 2018.<\/p>\n<p>12.\u00a0L.E. Buchanan, M.O. McAnally, N.L. Gruenke, G.C. Schatz, R.P. Van Duyne. \u201cStudying stimulated Raman activity in surface-enhanced femtosecond stimulated Raman spectroscopy by varying the excitation wavelength,\u201d <em>Journal of Physical Chemistry Letters<\/em>, 8, 3328-3333 (2017).<\/p>\n<p>11. L.E. Buchanan, N.L. Gruenke, M.O. McAnally, B. Negru, H.E. Mayhew, V.A. Apkarian, G.C. Schatz, R.P. Van Duyne. &#8220;Surface-enhanced femtosecond stimulated Raman spectroscopy 1 MHz repetition rates,\u201d <em>Journal of Physical Chemistry Letters<\/em>, 7, 4629-4634 (2016).<\/p>\n<p>10. A.W. Parker, T.O. Zhang, L.E. Buchanan, M.T. Zanni. &#8220;Insights into amylin aggregation by 2D IR spectroscopy,&#8221; <em>Biomedical Spectroscopy and Imaging<\/em>, 3, 189-96 (2014).<\/p>\n<p>9. L.E. Buchanan, J.K. Carr, A.M Fluitt, A.J. Hoganson, S.D. Moran, J.J. de Pablo, J.L. Skinner, M.T. Zanni. &#8220;Structural motif of polyglutamine amyloid fibrils discerned with mixed-isotope infrared spectroscopy,&#8221; <em>Proceedings of the National Academy of Sciences<\/em>, 111, 5796-5801 (2014).<\/p>\n<p>8. L.E. Buchanan, E.B. Dunkelberger, H.Q. Tran, P.-N. Cheng, C.-C. Chiu, P. Cao, D.P. Raleigh, J.J. dePablo , J.S. Nowick, M.T. Zanni, &#8220;Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient \u03b2-sheet,&#8221; <em>Proceedings of the National Academy of Sciences<\/em>, 110, 19285-90 (2013). *Highlighted in &#8220;Unfolding Diabetes,&#8221; <em>Chemical &amp; Engineering News<\/em>, 91 (46), 5 (2013).<\/p>\n<p>7. L. Wang, L.E. Buchanan, E.B. Dunkelberger, J.J. de Pablo, M.T. Zanni, J.L. Skinner, &#8220;Ultrafast Infrared Spectroscopy of Amylin Solution and Fibrils,&#8221; in <em>Ultrafast Infrared Vibrational Spectroscopy<\/em>, M.D. Fayer, Ed<em>.<\/em> CRC Press: Boca Raton, 437-460 (2013).<\/p>\n<p>6. J. Carr, L.E. Buchanan, M.T. Zanni, J.L. Skinner, &#8220;Structure and dynamics of urea\/water mixtures investigated by vibrational spectroscopy and molecular dynamics simulation,&#8221; <em>Journal of Physical Chemistry B<\/em>, <em>117<\/em>, 13291-300, (2013).<\/p>\n<p>5. E.B. Dunkelberger, L.E. Buchanan, P. Marek, P. Cao, D.P. Raleigh, M.T. Zanni, &#8220;Deamidation accelerates amyloid formation and alters amylin fiber structure,&#8221; <em>Journal of the American Chemical Society<\/em>, 134, 12658-67 (2012). *Highlighted in &#8220;Spectroscopic Technique Spots Effects of Deamidation on Proteins&#8221;, <em>Chemical &amp; Engineering News<\/em>, [online] July 6, 2012.<\/p>\n<p>4. S.D. Moran, A.M. Woys, L.E. Buchanan, E. Bixby, S.M. Decatur, M.T. Zanni, &#8220;Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human \u03b3D-crystallin amyloid fibrils,&#8221; <em>Proceedings of the National Academy of Sciences<\/em>, 109, 3329-34 (2012). *Highlighted in &#8220;Domain Structure of Cataract Amyloids,&#8221; <em>Chemical &amp; Engineering News<\/em>, 90 (7), 37 (2012).<\/p>\n<p>3. L.E. Buchanan, E.B. Dunkelberger, M.T. Zanni, &#8220;Examining amyloid structure and kinetics with 1D and 2D infrared spectroscopy and isotope labeling,&#8221; in <em>Protein Folding and Misfolding, <\/em>H. Fabian and D. Nauman, Eds. Springer: Heidelberg, 217-237 (2011).<\/p>\n<p>2. C.T. Middleton, L.E. Buchanan, E.B. Dunkelberger, M.T. Zanni, &#8220;Utilizing lifetimes to suppress random coil features in 2D IR spectra of peptides,&#8221; <em>Journal of Physical Chemistry Letters<\/em>, 2, 2357-2361 (2011).<\/p>\n<p><span style=\"font-size: 16.0016px\">1. A.S. Reddy, L. Wang, S. Singh, Y.L. Ling, <\/span>L. Buchanan<span style=\"font-size: 16.0016px\">, M.T. Zanni, J.L. Skinner, J.J. de Pablo, &#8220;Stable and metastable states of human amylin in solution,&#8221; <\/span><em style=\"font-family: inherit;font-size: 16.0016px\">Biophysical Journal<\/em><span style=\"font-size: 16.0016px\">, 99, 2208-16 (2010).<\/span><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Publications while at Vanderbilt University 19.\u00a0Kelsey Rochelle Webb, Kayla Anne Hess, Alisa Shmidt, Kathryn Diane Segner, Lauren Elizabeth Buchanan,\u00a0Probing local changes to \u03b1-helical structures with 2D IR spectroscopy and isotope labeling,\u00a0Biophysical Journal (2023), doi:\u00a0https:\/\/doi.org\/10.1016\/j.bpj.2023.03.014. 18.\u00a0Kayla A. Hess, Nathan J. Spear, Sophia A. Vogelsang, Janet E. Macdonald, and Lauren E. Buchanan , &#8220;Determining the impact of&#8230;<\/p>\n","protected":false},"author":6627,"featured_media":0,"parent":0,"menu_order":4,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"tags":[],"class_list":["post-26","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/my.dev.vanderbilt.edu\/buchanan\/wp-json\/wp\/v2\/pages\/26","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/my.dev.vanderbilt.edu\/buchanan\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/my.dev.vanderbilt.edu\/buchanan\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/my.dev.vanderbilt.edu\/buchanan\/wp-json\/wp\/v2\/users\/6627"}],"replies":[{"embeddable":true,"href":"https:\/\/my.dev.vanderbilt.edu\/buchanan\/wp-json\/wp\/v2\/comments?post=26"}],"version-history":[{"count":15,"href":"https:\/\/my.dev.vanderbilt.edu\/buchanan\/wp-json\/wp\/v2\/pages\/26\/revisions"}],"predecessor-version":[{"id":380,"href":"https:\/\/my.dev.vanderbilt.edu\/buchanan\/wp-json\/wp\/v2\/pages\/26\/revisions\/380"}],"wp:attachment":[{"href":"https:\/\/my.dev.vanderbilt.edu\/buchanan\/wp-json\/wp\/v2\/media?parent=26"}],"wp:term":[{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/my.dev.vanderbilt.edu\/buchanan\/wp-json\/wp\/v2\/tags?post=26"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}