Shedding light on protein folding, structural and functional dynamics by single molecule studies

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Shedding light on protein folding, structural and functional dynamics by single molecule studies. / Bavishi, Krutika; Hatzakis, Nikos.

In: Molecules, Vol. 19, No. 12, 2014, p. 19407-19434.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Bavishi, K & Hatzakis, N 2014, 'Shedding light on protein folding, structural and functional dynamics by single molecule studies', Molecules, vol. 19, no. 12, pp. 19407-19434. https://doi.org/10.3390/molecules191219407

APA

Bavishi, K., & Hatzakis, N. (2014). Shedding light on protein folding, structural and functional dynamics by single molecule studies. Molecules, 19(12), 19407-19434. https://doi.org/10.3390/molecules191219407

Vancouver

Bavishi K, Hatzakis N. Shedding light on protein folding, structural and functional dynamics by single molecule studies. Molecules. 2014;19(12):19407-19434. https://doi.org/10.3390/molecules191219407

Author

Bavishi, Krutika ; Hatzakis, Nikos. / Shedding light on protein folding, structural and functional dynamics by single molecule studies. In: Molecules. 2014 ; Vol. 19, No. 12. pp. 19407-19434.

Bibtex

@article{b036c00994fc4193af49c37d9d31fb4c,
title = "Shedding light on protein folding, structural and functional dynamics by single molecule studies",
abstract = "The advent of advanced single molecule measurements unveiled a great wealth of dynamic information revolutionizing our understanding of protein dynamics and behavior in ways unattainable by conventional bulk assays. Equipped with the ability to record distribution of behaviors rather than the mean property of a population, single molecule measurements offer observation and quantification of the abundance, lifetime and function of multiple protein states. They also permit the direct observation of the transient and rarely populated intermediates in the energy landscape that are typically averaged out in non-synchronized ensemble measurements. Single molecule studies have thus provided novel insights about how the dynamic sampling of the free energy landscape dictates all aspects of protein behavior; from its folding to function. Here we will survey some of the state of the art contributions in deciphering mechanisms that underlie protein folding, structural and functional dynamics by single molecule fluorescence microscopy techniques. We will discuss a few selected examples highlighting the power of the emerging techniques and finally discuss the future improvements and directions.",
keywords = "Allosteric regulation, Conformational dynamics, Free energy landscape, Protein folding, Single molecule FRET, Single molecules",
author = "Krutika Bavishi and Nikos Hatzakis",
year = "2014",
doi = "10.3390/molecules191219407",
language = "English",
volume = "19",
pages = "19407--19434",
journal = "Molecules",
issn = "1420-3049",
publisher = "M D P I AG",
number = "12",

}

RIS

TY - JOUR

T1 - Shedding light on protein folding, structural and functional dynamics by single molecule studies

AU - Bavishi, Krutika

AU - Hatzakis, Nikos

PY - 2014

Y1 - 2014

N2 - The advent of advanced single molecule measurements unveiled a great wealth of dynamic information revolutionizing our understanding of protein dynamics and behavior in ways unattainable by conventional bulk assays. Equipped with the ability to record distribution of behaviors rather than the mean property of a population, single molecule measurements offer observation and quantification of the abundance, lifetime and function of multiple protein states. They also permit the direct observation of the transient and rarely populated intermediates in the energy landscape that are typically averaged out in non-synchronized ensemble measurements. Single molecule studies have thus provided novel insights about how the dynamic sampling of the free energy landscape dictates all aspects of protein behavior; from its folding to function. Here we will survey some of the state of the art contributions in deciphering mechanisms that underlie protein folding, structural and functional dynamics by single molecule fluorescence microscopy techniques. We will discuss a few selected examples highlighting the power of the emerging techniques and finally discuss the future improvements and directions.

AB - The advent of advanced single molecule measurements unveiled a great wealth of dynamic information revolutionizing our understanding of protein dynamics and behavior in ways unattainable by conventional bulk assays. Equipped with the ability to record distribution of behaviors rather than the mean property of a population, single molecule measurements offer observation and quantification of the abundance, lifetime and function of multiple protein states. They also permit the direct observation of the transient and rarely populated intermediates in the energy landscape that are typically averaged out in non-synchronized ensemble measurements. Single molecule studies have thus provided novel insights about how the dynamic sampling of the free energy landscape dictates all aspects of protein behavior; from its folding to function. Here we will survey some of the state of the art contributions in deciphering mechanisms that underlie protein folding, structural and functional dynamics by single molecule fluorescence microscopy techniques. We will discuss a few selected examples highlighting the power of the emerging techniques and finally discuss the future improvements and directions.

KW - Allosteric regulation

KW - Conformational dynamics

KW - Free energy landscape

KW - Protein folding

KW - Single molecule FRET

KW - Single molecules

U2 - 10.3390/molecules191219407

DO - 10.3390/molecules191219407

M3 - Journal article

C2 - 25429564

AN - SCOPUS:84919756005

VL - 19

SP - 19407

EP - 19434

JO - Molecules

JF - Molecules

SN - 1420-3049

IS - 12

ER -

ID: 130979845