Insight into the structure and the mechanism of the slow proton transfer in the GFP double mutant T203V/S205A (Q27690114)

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16 March 2020

title

Insight into the structure and the mechanism of the slow proton transfer in the GFP double mutant T203V/S205A (English)

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16 March 2020

2

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16 March 2020

author name string

Vered Wineman-Fisher

1

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16 March 2020

Shay Shomer

3

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16 March 2020

Rinat Gepshtein

4

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16 March 2020

Dan Huppert

5

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16 March 2020

Mari Saif

6

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16 March 2020

Karen Kallio

7

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S James Remington

8

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16 March 2020

Yifat Miller

9

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language of work or name

English

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publication date

28 April 2014

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Physical Chemistry Chemical Physics

16 March 2020

published in

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16 March 2020

volume

16

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16 March 2020

issue

23

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page(s)

11196-11208

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Primary structure of the Aequorea victoria green-fluorescent protein

16 March 2020

cites work

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Ultrafast Electronic and Vibrational Dynamics of Stabilized A State Mutants of the Green Fluorescent Protein (GFP): Snipping the Proton Wire

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Observation of excited-state proton transfer in green fluorescent protein using ultrafast vibrational spectroscopy.

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An alternative excited-state proton transfer pathway in green fluorescent protein variant S205V

21 January 2018

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Proton transfer in wild-type GFP and S205V mutant is reduced by conformational changes of residues in the proton wire.

21 January 2018

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21 January 2018

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Ultrafast proton transfer to solvent: molecularity and intermediates from solvation- and diffusion-controlled regimes.

21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1039/C4CP00311J

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16 March 2020

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