{"id":{"repo_id":"mit","oai_identifier":"oai:dspace.mit.edu:1721.1/112444"},"canonical_url":"https://search.dev.ndltd.org/etd/mit/oai:dspace.mit.edu:1721.1/112444","repository":{"repo_id":"mit","name":"MIT","base_url":"https://dspace.mit.edu/oai/request"},"display":{"title":"Membrane and membrane protein dynamics studied with time-resolved infrared spectroscopy","abstract":"Proteins are the machinery of the cell, performing functions essential for life. Proteins do not operate in isolation, however. Their function is intimately coupled to their environment; changes in this environment modulate the behavior of the protein. One of the most striking examples of protein-environment coupling is the interaction between membrane proteins and membranes. These interactions govern some of the most fundamental processes in biology, yet the origins of protein-membrane coupling are not well understood. Infrared (IR) spectroscopy offers a route to non-invasively probing these interactions. However, despite sustained interest in the problem over many decades, only limited progress has been made using IR spectroscopy to study protein-membrane interactions. One of the main reasons for this is the density of information encoded into a small frequency range - many hundreds of oscillators may contribute to a signal which spans a <100 cm-¹ range. This spectral congestion may be relieved by spreading the information over an additional axis - an additional frequency axis in the case of multidimensional IR spectroscopy, or over a kinetic axis in transient relaxation experiments. The temporal information encoded by multidimensional IR spectroscopy and transient experiments also provides a route to studying the dynamics of membranes and membrane proteins over a range of timescales, from sub-picoseconds to milliseconds. The combination of structural and temporal information afforded by IR spectroscopy offers the possibility of developing a truly dynamic picture of membranes and membrane proteins. This thesis details efforts to first develop an understanding of what information is contained within the IR spectrum of biologically-native carbonyl groups, and then use this understanding to develop a picture of what fluctuations occur in membranes on the sub-nanosecond, sub-nanometer time- and length-scales. Interactions between membranes and membrane proteins are probed further by utilizing a rapid temperature-jump to induce a phase transition in the membrane. The response of the membrane, and membrane protein, to this phase transition reveals a picture of conformational change in a membrane protein slaved to the dynamics of the membrane.","abstract_html":"Proteins are the machinery of the cell, performing functions essential for life. Proteins do not operate in isolation, however. Their function is intimately coupled to their environment; changes in this environment modulate the behavior of the protein. One of the most striking examples of protein-environment coupling is the interaction between membrane proteins and membranes. These interactions govern some of the most fundamental processes in biology, yet the origins of protein-membrane coupling are not well understood. Infrared (IR) spectroscopy offers a route to non-invasively probing these interactions. However, despite sustained interest in the problem over many decades, only limited progress has been made using IR spectroscopy to study protein-membrane interactions. One of the main reasons for this is the density of information encoded into a small frequency range - many hundreds of oscillators may contribute to a signal which spans a &lt;100 cm-¹ range. This spectral congestion may be relieved by spreading the information over an additional axis - an additional frequency axis in the case of multidimensional IR spectroscopy, or over a kinetic axis in transient relaxation experiments. The temporal information encoded by multidimensional IR spectroscopy and transient experiments also provides a route to studying the dynamics of membranes and membrane proteins over a range of timescales, from sub-picoseconds to milliseconds. The combination of structural and temporal information afforded by IR spectroscopy offers the possibility of developing a truly dynamic picture of membranes and membrane proteins. This thesis details efforts to first develop an understanding of what information is contained within the IR spectrum of biologically-native carbonyl groups, and then use this understanding to develop a picture of what fluctuations occur in membranes on the sub-nanosecond, sub-nanometer time- and length-scales. Interactions between membranes and membrane proteins are probed further by utilizing a rapid temperature-jump to induce a phase transition in the membrane. The response of the membrane, and membrane protein, to this phase transition reveals a picture of conformational change in a membrane protein slaved to the dynamics of the membrane.","abstract_has_math":false,"creators":["Stevenson, Paul, Ph. D. Massachusetts Institute of Technology"],"institution":"Massachusetts Institute of Technology","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":"Massachusetts Institute of Technology. Department of Chemistry.","school":null,"contributors":[],"advisors":["Andrei Tokmakoff."],"committee_chairs":[],"committee_members":[],"year":2017,"date_issued":"2017","date_published":"2017","updated_at":"2026-07-22T22:20:57Z","subjects":["Chemistry."],"languages":["eng"],"rights":["MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission."],"rights_urls":["http://dspace.mit.edu/handle/1721.1/7582"],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/1721.1/112444","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Andrei Tokmakoff."]},{"key":"dc:contributor.department","label":"Department","values":["Massachusetts Institute of Technology. Department of Chemistry."]},{"key":"dc:contributor.other","label":"Dc Contributor Other","values":["Massachusetts Institute of Technology. Department of Chemistry."]},{"key":"dc:creator","label":"Author","values":["Stevenson, Paul, Ph. D. 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They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission."]},{"key":"dc:rights.uri","label":"Rights URI","values":["http://dspace.mit.edu/handle/1721.1/7582"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/1721.1/112444"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Thesis: Ph. D. in Physical Chemistry, Massachusetts Institute of Technology, Department of Chemistry, 2017.","Cataloged from PDF version of thesis.","Includes bibliographical references (pages 281-307)."]},{"key":"dc:description.abstract","label":"Abstract","values":["Proteins are the machinery of the cell, performing functions essential for life. Proteins do not operate in isolation, however. Their function is intimately coupled to their environment; changes in this environment modulate the behavior of the protein. One of the most striking examples of protein-environment coupling is the interaction between membrane proteins and membranes. These interactions govern some of the most fundamental processes in biology, yet the origins of protein-membrane coupling are not well understood. Infrared (IR) spectroscopy offers a route to non-invasively probing these interactions. However, despite sustained interest in the problem over many decades, only limited progress has been made using IR spectroscopy to study protein-membrane interactions. One of the main reasons for this is the density of information encoded into a small frequency range - many hundreds of oscillators may contribute to a signal which spans a <100 cm-¹ range. This spectral congestion may be relieved by spreading the information over an additional axis - an additional frequency axis in the case of multidimensional IR spectroscopy, or over a kinetic axis in transient relaxation experiments. The temporal information encoded by multidimensional IR spectroscopy and transient experiments also provides a route to studying the dynamics of membranes and membrane proteins over a range of timescales, from sub-picoseconds to milliseconds. The combination of structural and temporal information afforded by IR spectroscopy offers the possibility of developing a truly dynamic picture of membranes and membrane proteins. This thesis details efforts to first develop an understanding of what information is contained within the IR spectrum of biologically-native carbonyl groups, and then use this understanding to develop a picture of what fluctuations occur in membranes on the sub-nanosecond, sub-nanometer time- and length-scales. Interactions between membranes and membrane proteins are probed further by utilizing a rapid temperature-jump to induce a phase transition in the membrane. The response of the membrane, and membrane protein, to this phase transition reveals a picture of conformational change in a membrane protein slaved to the dynamics of the membrane."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Ph. D. in Physical Chemistry"]},{"key":"dc:title","label":"Title","values":["Membrane and membrane protein dynamics studied with time-resolved infrared spectroscopy"]}]}],"canonical_facts":{"dc:contributor.advisor":["Andrei Tokmakoff."],"dc:contributor.department":["Massachusetts Institute of Technology. Department of Chemistry."],"dc:contributor.other":["Massachusetts Institute of Technology. Department of Chemistry."],"dc:creator":["Stevenson, Paul, Ph. D. Massachusetts Institute of Technology"],"dc:date.accessioned":["2017-12-05T19:13:05Z"],"dc:date.available":["2017-12-05T19:13:05Z"],"dc:date.issued":["2017"],"dc:description":["Thesis: Ph. D. in Physical Chemistry, Massachusetts Institute of Technology, Department of Chemistry, 2017.","Cataloged from PDF version of thesis.","Includes bibliographical references (pages 281-307)."],"dc:description.abstract":["Proteins are the machinery of the cell, performing functions essential for life. Proteins do not operate in isolation, however. Their function is intimately coupled to their environment; changes in this environment modulate the behavior of the protein. One of the most striking examples of protein-environment coupling is the interaction between membrane proteins and membranes. These interactions govern some of the most fundamental processes in biology, yet the origins of protein-membrane coupling are not well understood. Infrared (IR) spectroscopy offers a route to non-invasively probing these interactions. However, despite sustained interest in the problem over many decades, only limited progress has been made using IR spectroscopy to study protein-membrane interactions. One of the main reasons for this is the density of information encoded into a small frequency range - many hundreds of oscillators may contribute to a signal which spans a <100 cm-¹ range. This spectral congestion may be relieved by spreading the information over an additional axis - an additional frequency axis in the case of multidimensional IR spectroscopy, or over a kinetic axis in transient relaxation experiments. The temporal information encoded by multidimensional IR spectroscopy and transient experiments also provides a route to studying the dynamics of membranes and membrane proteins over a range of timescales, from sub-picoseconds to milliseconds. The combination of structural and temporal information afforded by IR spectroscopy offers the possibility of developing a truly dynamic picture of membranes and membrane proteins. This thesis details efforts to first develop an understanding of what information is contained within the IR spectrum of biologically-native carbonyl groups, and then use this understanding to develop a picture of what fluctuations occur in membranes on the sub-nanosecond, sub-nanometer time- and length-scales. Interactions between membranes and membrane proteins are probed further by utilizing a rapid temperature-jump to induce a phase transition in the membrane. The response of the membrane, and membrane protein, to this phase transition reveals a picture of conformational change in a membrane protein slaved to the dynamics of the membrane."],"dc:description.degree":["Ph. D. in Physical Chemistry"],"dc:identifier.uri":["http://hdl.handle.net/1721.1/112444"],"dc:language.iso":["eng"],"dc:publisher":["Massachusetts Institute of Technology"],"dc:rights":["MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission."],"dc:rights.uri":["http://dspace.mit.edu/handle/1721.1/7582"],"dc:subject":["Chemistry."],"dc:title":["Membrane and membrane protein dynamics studied with time-resolved infrared spectroscopy"],"dc:type":["Thesis"]},"updated_at":"2026-07-22T22:20:57Z"}