Abstract
As more and more proteins specific to hair cells are discovered, it becomes imperative to understand their structure and how that contributes to their function. The fluorescence microscopic methods described here can be employed to provide information on protein-protein interactions, whether homomeric or heteromeric, and on protein conformation. Here, we describe two fluorescence microscopic methodologies applied to the outer hair cell-specific membrane protein prestin: the intensity and fluorescence lifetime (FLIM) variants of FRET (Fluorescence Resonance Energy Transfer), used in the study of protein-protein interactions, and the Scanning Cysteine Accessibility Method (SCAM), used for the determination of protein conformation. The methods are readily adaptable to other proteins.
| Original language | English |
|---|---|
| Title of host publication | Auditory and Vestibular Research: Methods and Protocols |
| Publisher | Humana Press |
| Pages | 369-379 |
| Number of pages | 11 |
| Volume | 493 |
| ISBN (Print) | 9781934115626 |
| DOIs | |
| State | Published - 2009 |
Publication series
| Name | Methods in Molecular Biology |
|---|---|
| Volume | 493 |
| ISSN (Print) | 10643745 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Genetics
Cite this
Fluorescence microscopy methods in the study of protein structure and function. / Jensen-Smith, Heather; Currall, Benjamin; Rossino, Danielle; Tiede, Leann; Nichols, Michael G.; Hallworth, Richard J.
Auditory and Vestibular Research: Methods and Protocols. Vol. 493 Humana Press, 2009. p. 369-379 (Methods in Molecular Biology; Vol. 493).Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Fluorescence microscopy methods in the study of protein structure and function
AU - Jensen-Smith, Heather
AU - Currall, Benjamin
AU - Rossino, Danielle
AU - Tiede, Leann
AU - Nichols, Michael G.
AU - Hallworth, Richard J.
PY - 2009
Y1 - 2009
N2 - As more and more proteins specific to hair cells are discovered, it becomes imperative to understand their structure and how that contributes to their function. The fluorescence microscopic methods described here can be employed to provide information on protein-protein interactions, whether homomeric or heteromeric, and on protein conformation. Here, we describe two fluorescence microscopic methodologies applied to the outer hair cell-specific membrane protein prestin: the intensity and fluorescence lifetime (FLIM) variants of FRET (Fluorescence Resonance Energy Transfer), used in the study of protein-protein interactions, and the Scanning Cysteine Accessibility Method (SCAM), used for the determination of protein conformation. The methods are readily adaptable to other proteins.
AB - As more and more proteins specific to hair cells are discovered, it becomes imperative to understand their structure and how that contributes to their function. The fluorescence microscopic methods described here can be employed to provide information on protein-protein interactions, whether homomeric or heteromeric, and on protein conformation. Here, we describe two fluorescence microscopic methodologies applied to the outer hair cell-specific membrane protein prestin: the intensity and fluorescence lifetime (FLIM) variants of FRET (Fluorescence Resonance Energy Transfer), used in the study of protein-protein interactions, and the Scanning Cysteine Accessibility Method (SCAM), used for the determination of protein conformation. The methods are readily adaptable to other proteins.
UR - http://www.scopus.com/inward/record.url?scp=84934444617&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84934444617&partnerID=8YFLogxK
U2 - 10.1007/978-1-59745-523-7_22
DO - 10.1007/978-1-59745-523-7_22
M3 - Chapter
SN - 9781934115626
VL - 493
T3 - Methods in Molecular Biology
SP - 369
EP - 379
BT - Auditory and Vestibular Research: Methods and Protocols
PB - Humana Press
ER -