Current Protocols in Neuroscience: Fluorescence Recovery after Photobleaching (FRAP) with a Focus on F-Actin

Lori R. Hardy; Lori Redmond

Current Protocols in Neuroscience: Fluorescence Recovery after Photobleaching (FRAP) with a Focus on F-Actin

Research output: Book/Report › Book

Abstract

In this unit on fluorescence recovery after photobleaching (FRAP), an imaging approach to study protein-protein interactions in situ is described. The protocols presented use confocal microscopy to examine the mobility of a fluorescent protein by measuring the recovery of the protein in a bleached area. The data gained in FRAP studies is qualitative and yields insight into relative binding affinity, binding characteristics, and the effect of treatments or mutations on protein mobility.

Original language	American English
Publisher	Current Protocols in Neuroscience
Volume	Chapter 2
State	Published - Jan 1 2012

Keywords

FRAP
actin
protein mobility
GFPactin cytoskeleton
actins
cells
cultured
fluorescence recovery after photobleaching
green fluorescent proteins
microscopy
confocal
time factors

Disciplines

Medicine and Health Sciences
Neurology
Neurosciences

Cite this

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abstract = " In this unit on fluorescence recovery after photobleaching (FRAP), an imaging approach to study protein-protein interactions in situ is described. The protocols presented use confocal microscopy to examine the mobility of a fluorescent protein by measuring the recovery of the protein in a bleached area. The data gained in FRAP studies is qualitative and yields insight into relative binding affinity, binding characteristics, and the effect of treatments or mutations on protein mobility.",

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AU - Redmond, Lori

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N2 - In this unit on fluorescence recovery after photobleaching (FRAP), an imaging approach to study protein-protein interactions in situ is described. The protocols presented use confocal microscopy to examine the mobility of a fluorescent protein by measuring the recovery of the protein in a bleached area. The data gained in FRAP studies is qualitative and yields insight into relative binding affinity, binding characteristics, and the effect of treatments or mutations on protein mobility.

AB - In this unit on fluorescence recovery after photobleaching (FRAP), an imaging approach to study protein-protein interactions in situ is described. The protocols presented use confocal microscopy to examine the mobility of a fluorescent protein by measuring the recovery of the protein in a bleached area. The data gained in FRAP studies is qualitative and yields insight into relative binding affinity, binding characteristics, and the effect of treatments or mutations on protein mobility.

KW - FRAP

KW - actin

KW - protein mobility

KW - GFPactin cytoskeleton

KW - actins

KW - cells

KW - cultured

KW - fluorescence recovery after photobleaching

KW - green fluorescent proteins

KW - microscopy

KW - confocal

KW - time factors

UR - https://digitalcommons.pcom.edu/scholarly_papers/196

M3 - Book

VL - Chapter 2

BT - Current Protocols in Neuroscience

PB - Current Protocols in Neuroscience

ER -

Current Protocols in Neuroscience: Fluorescence Recovery after Photobleaching (FRAP) with a Focus on F-Actin

Abstract

Keywords

Disciplines

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Cite this