Short-Range Distance Measurement by Transition Metal Ion FRET

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Standard

Short-Range Distance Measurement by Transition Metal Ion FRET. / Mortensen, Jonas S.; Loland, Claus J.

Biophysics of membrane proteins. Humana Press, 2020. p. 299-311 (Methods in Molecular Biology, Vol. 2168).

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Harvard

Mortensen, JS & Loland, CJ 2020, Short-Range Distance Measurement by Transition Metal Ion FRET. in Biophysics of membrane proteins. Humana Press, Methods in Molecular Biology, vol. 2168, pp. 299-311. https://doi.org/10.1007/978-1-0716-0724-4_14

APA

Mortensen, J. S., & Loland, C. J. (2020). Short-Range Distance Measurement by Transition Metal Ion FRET. In Biophysics of membrane proteins (pp. 299-311). Humana Press. Methods in Molecular Biology Vol. 2168 https://doi.org/10.1007/978-1-0716-0724-4_14

Vancouver

Mortensen JS, Loland CJ. Short-Range Distance Measurement by Transition Metal Ion FRET. In Biophysics of membrane proteins. Humana Press. 2020. p. 299-311. (Methods in Molecular Biology, Vol. 2168). https://doi.org/10.1007/978-1-0716-0724-4_14

Author

Mortensen, Jonas S. ; Loland, Claus J. / Short-Range Distance Measurement by Transition Metal Ion FRET. Biophysics of membrane proteins. Humana Press, 2020. pp. 299-311 (Methods in Molecular Biology, Vol. 2168).

Bibtex

@inbook{883a018d6bba4bd2b0a1fcc01f67894d,
title = "Short-Range Distance Measurement by Transition Metal Ion FRET",
abstract = "Measurement of atomic-scale conformational dynamics in proteins has proved a challenging endeavor, although these movements are pivotal for understanding the mechanisms behind protein function. Herein we describe a fluorescence-based method that enables the measurement of distances between specific domains within a protein and how it might change during protein function. The method is transition metal ion F{\"o}rster resonance energy transfer (tmFRET) and builds on the principle that the fluorescence emission from a fluorophore can be quenched in a distance-dependent manner by a colored transition metal such as nickel (Ni2+), copper (Cu2+), or cobalt (Co2+). It can be applied to literally any protein where it is possible to perform site-specific incorporation of a fluorescent molecule. This chapter will explain the use and applications of tmFRET in detail using incorporation of the dye with cysteine chemistry on a purified protein sample.",
keywords = "Conformational dynamics, Cysteine chemistry, Fluorescence spectroscopy, F{\"o}rster resonance energy transfer, Intramolecular distance measurements, Protein purification, Transition metals",
author = "Mortensen, {Jonas S.} and Loland, {Claus J.}",
year = "2020",
doi = "10.1007/978-1-0716-0724-4_14",
language = "English",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
pages = "299--311",
booktitle = "Biophysics of membrane proteins",
address = "United States",

}

RIS

TY - CHAP

T1 - Short-Range Distance Measurement by Transition Metal Ion FRET

AU - Mortensen, Jonas S.

AU - Loland, Claus J.

PY - 2020

Y1 - 2020

N2 - Measurement of atomic-scale conformational dynamics in proteins has proved a challenging endeavor, although these movements are pivotal for understanding the mechanisms behind protein function. Herein we describe a fluorescence-based method that enables the measurement of distances between specific domains within a protein and how it might change during protein function. The method is transition metal ion Förster resonance energy transfer (tmFRET) and builds on the principle that the fluorescence emission from a fluorophore can be quenched in a distance-dependent manner by a colored transition metal such as nickel (Ni2+), copper (Cu2+), or cobalt (Co2+). It can be applied to literally any protein where it is possible to perform site-specific incorporation of a fluorescent molecule. This chapter will explain the use and applications of tmFRET in detail using incorporation of the dye with cysteine chemistry on a purified protein sample.

AB - Measurement of atomic-scale conformational dynamics in proteins has proved a challenging endeavor, although these movements are pivotal for understanding the mechanisms behind protein function. Herein we describe a fluorescence-based method that enables the measurement of distances between specific domains within a protein and how it might change during protein function. The method is transition metal ion Förster resonance energy transfer (tmFRET) and builds on the principle that the fluorescence emission from a fluorophore can be quenched in a distance-dependent manner by a colored transition metal such as nickel (Ni2+), copper (Cu2+), or cobalt (Co2+). It can be applied to literally any protein where it is possible to perform site-specific incorporation of a fluorescent molecule. This chapter will explain the use and applications of tmFRET in detail using incorporation of the dye with cysteine chemistry on a purified protein sample.

KW - Conformational dynamics

KW - Cysteine chemistry

KW - Fluorescence spectroscopy

KW - Förster resonance energy transfer

KW - Intramolecular distance measurements

KW - Protein purification

KW - Transition metals

UR - http://www.scopus.com/inward/record.url?scp=85101445057&partnerID=8YFLogxK

U2 - 10.1007/978-1-0716-0724-4_14

DO - 10.1007/978-1-0716-0724-4_14

M3 - Book chapter

C2 - 33582998

AN - SCOPUS:85101445057

T3 - Methods in Molecular Biology

SP - 299

EP - 311

BT - Biophysics of membrane proteins

PB - Humana Press

ER -

ID: 270666372