Inertial water response dominates protein solvation dynamics

Laurie A. Bizimana; Jordan Epstein; Daniel B. Turner

doi:10.1016/j.cplett.2019.04.069

Inertial water response dominates protein solvation dynamics

Laurie A. Bizimana, Jordan Epstein, Daniel B. Turner

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Establishing the mechanism of protein folding and other physiological processes requires a detailed comprehension of protein-solvent interactions. The fastest protein solvation dynamics have not yet been thoroughly investigated due to challenges associated with controlling few-cycle laser pulses and identifying ideal model systems. Here we use 6 fs laser pulses to quantify the sub-picosecond solvation dynamics of an engineered pigment-protein complex that serves as an ideal probe of solvation dynamics. The data reveal that protein solvation dynamics are described well by a single lifetime of 33 fs, indicating that the mechanism of protein solvation is dominated by the inertial water component.

Original language	English (US)
Pages (from-to)	1-5
Number of pages	5
Journal	Chemical Physics Letters
Volume	728
DOIs	https://doi.org/10.1016/j.cplett.2019.04.069
State	Published - Aug 2019

ASJC Scopus subject areas

General Physics and Astronomy
Physical and Theoretical Chemistry

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10.1016/j.cplett.2019.04.069

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title = "Inertial water response dominates protein solvation dynamics",

abstract = "Establishing the mechanism of protein folding and other physiological processes requires a detailed comprehension of protein-solvent interactions. The fastest protein solvation dynamics have not yet been thoroughly investigated due to challenges associated with controlling few-cycle laser pulses and identifying ideal model systems. Here we use 6 fs laser pulses to quantify the sub-picosecond solvation dynamics of an engineered pigment-protein complex that serves as an ideal probe of solvation dynamics. The data reveal that protein solvation dynamics are described well by a single lifetime of 33 fs, indicating that the mechanism of protein solvation is dominated by the inertial water component.",

author = "Bizimana, {Laurie A.} and Jordan Epstein and Turner, {Daniel B.}",

note = "Funding Information: This work was supported by the National Science Foundation [CAREER Grant No. CHE-1552235, and a Graduate Research Fellowship to LAB]and by the Alfred P. Sloan Foundation. We thank J. Clark Lagarias for providing the initial PCB-Cph1Δ sample and Casey Reed for assistance with protein production and purification. Funding Information: This work was supported by the National Science Foundation [CAREER Grant No. CHE-1552235 , and a Graduate Research Fellowship to LAB] and by the Alfred P. Sloan Foundation. We thank J. Clark Lagarias for providing the initial PCB-Cph1 Δ sample and Casey Reed for assistance with protein production and purification. Publisher Copyright: {\textcopyright} 2019 Elsevier B.V.",

year = "2019",

month = aug,

doi = "10.1016/j.cplett.2019.04.069",

language = "English (US)",

volume = "728",

pages = "1--5",

journal = "Chemical Physics Letters",

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AU - Bizimana, Laurie A.

AU - Epstein, Jordan

AU - Turner, Daniel B.

N1 - Funding Information: This work was supported by the National Science Foundation [CAREER Grant No. CHE-1552235, and a Graduate Research Fellowship to LAB]and by the Alfred P. Sloan Foundation. We thank J. Clark Lagarias for providing the initial PCB-Cph1Δ sample and Casey Reed for assistance with protein production and purification. Funding Information: This work was supported by the National Science Foundation [CAREER Grant No. CHE-1552235 , and a Graduate Research Fellowship to LAB] and by the Alfred P. Sloan Foundation. We thank J. Clark Lagarias for providing the initial PCB-Cph1 Δ sample and Casey Reed for assistance with protein production and purification. Publisher Copyright: © 2019 Elsevier B.V.

PY - 2019/8

Y1 - 2019/8

N2 - Establishing the mechanism of protein folding and other physiological processes requires a detailed comprehension of protein-solvent interactions. The fastest protein solvation dynamics have not yet been thoroughly investigated due to challenges associated with controlling few-cycle laser pulses and identifying ideal model systems. Here we use 6 fs laser pulses to quantify the sub-picosecond solvation dynamics of an engineered pigment-protein complex that serves as an ideal probe of solvation dynamics. The data reveal that protein solvation dynamics are described well by a single lifetime of 33 fs, indicating that the mechanism of protein solvation is dominated by the inertial water component.

AB - Establishing the mechanism of protein folding and other physiological processes requires a detailed comprehension of protein-solvent interactions. The fastest protein solvation dynamics have not yet been thoroughly investigated due to challenges associated with controlling few-cycle laser pulses and identifying ideal model systems. Here we use 6 fs laser pulses to quantify the sub-picosecond solvation dynamics of an engineered pigment-protein complex that serves as an ideal probe of solvation dynamics. The data reveal that protein solvation dynamics are described well by a single lifetime of 33 fs, indicating that the mechanism of protein solvation is dominated by the inertial water component.

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JO - Chemical Physics Letters

JF - Chemical Physics Letters

ER -

Inertial water response dominates protein solvation dynamics

Abstract

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