Du er her: » Contemporary NMR Studies of Protein Electrostatics

Contemporary NMR Studies of Protein Electrostatics

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Standard

Contemporary NMR Studies of Protein Electrostatics. / Hass, Mathias A S; Mulder, Frans A A.

I: Annual Review of Biophysics, Bind 44, 22.06.2015, s. 53-75.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Harvard

Hass, MAS & Mulder, FAA 2015, 'Contemporary NMR Studies of Protein Electrostatics', Annual Review of Biophysics, bind 44, s. 53-75. https://doi.org/10.1146/annurev-biophys-083012-130351

APA

Hass, M. A. S., & Mulder, F. A. A. (2015). Contemporary NMR Studies of Protein Electrostatics. Annual Review of Biophysics, 44, 53-75. https://doi.org/10.1146/annurev-biophys-083012-130351

CBE

Hass MAS, Mulder FAA. 2015. Contemporary NMR Studies of Protein Electrostatics. Annual Review of Biophysics. 44:53-75. https://doi.org/10.1146/annurev-biophys-083012-130351

MLA

Hass, Mathias A S og Frans A A Mulder. "Contemporary NMR Studies of Protein Electrostatics". Annual Review of Biophysics. 2015, 44. 53-75. https://doi.org/10.1146/annurev-biophys-083012-130351

Vancouver

Hass MAS, Mulder FAA. Contemporary NMR Studies of Protein Electrostatics. Annual Review of Biophysics. 2015 jun 22;44:53-75. https://doi.org/10.1146/annurev-biophys-083012-130351

Author

Hass, Mathias A S ; Mulder, Frans A A. / Contemporary NMR Studies of Protein Electrostatics. I: Annual Review of Biophysics. 2015 ; Bind 44. s. 53-75.

Bibtex

@article{3f30740ee0584dafa478da651378864e,
title = "Contemporary NMR Studies of Protein Electrostatics",
abstract = "Electrostatics play an important role in many aspects of protein chemistry. However, the accurate determination of side chain proton affinity in proteins by experiment and theory remains challenging. In recent years the field of nuclear magnetic resonance spectroscopy has advanced the way that protonation states are measured, allowing researchers to examine electrostatic interactions at an unprecedented level of detail and accuracy. Experiments are now in place that follow pH-dependent (13)C and (15)N chemical shifts as spatially close as possible to the sites of protonation, allowing all titratable amino acid side chains to be probed sequence specifically. The strong and telling response of carefully selected reporter nuclei allows individual titration events to be monitored. At the same time, improved frameworks allow researchers to model multiple coupled protonation equilibria and to identify the underlying pH-dependent contributions to the chemical shifts.",
author = "Hass, {Mathias A S} and Mulder, {Frans A A}",
year = "2015",
month = "6",
day = "22",
doi = "10.1146/annurev-biophys-083012-130351",
language = "English",
volume = "44",
pages = "53--75",
journal = "Annual Review of Biophysics",
issn = "1936-122X",
publisher = "Annual Reviews",

}

RIS

TY - JOUR

T1 - Contemporary NMR Studies of Protein Electrostatics

AU - Hass, Mathias A S

AU - Mulder, Frans A A

PY - 2015/6/22

Y1 - 2015/6/22

N2 - Electrostatics play an important role in many aspects of protein chemistry. However, the accurate determination of side chain proton affinity in proteins by experiment and theory remains challenging. In recent years the field of nuclear magnetic resonance spectroscopy has advanced the way that protonation states are measured, allowing researchers to examine electrostatic interactions at an unprecedented level of detail and accuracy. Experiments are now in place that follow pH-dependent (13)C and (15)N chemical shifts as spatially close as possible to the sites of protonation, allowing all titratable amino acid side chains to be probed sequence specifically. The strong and telling response of carefully selected reporter nuclei allows individual titration events to be monitored. At the same time, improved frameworks allow researchers to model multiple coupled protonation equilibria and to identify the underlying pH-dependent contributions to the chemical shifts.

AB - Electrostatics play an important role in many aspects of protein chemistry. However, the accurate determination of side chain proton affinity in proteins by experiment and theory remains challenging. In recent years the field of nuclear magnetic resonance spectroscopy has advanced the way that protonation states are measured, allowing researchers to examine electrostatic interactions at an unprecedented level of detail and accuracy. Experiments are now in place that follow pH-dependent (13)C and (15)N chemical shifts as spatially close as possible to the sites of protonation, allowing all titratable amino acid side chains to be probed sequence specifically. The strong and telling response of carefully selected reporter nuclei allows individual titration events to be monitored. At the same time, improved frameworks allow researchers to model multiple coupled protonation equilibria and to identify the underlying pH-dependent contributions to the chemical shifts.

U2 - 10.1146/annurev-biophys-083012-130351

DO - 10.1146/annurev-biophys-083012-130351

M3 - Journal article

VL - 44

SP - 53

EP - 75

JO - Annual Review of Biophysics

JF - Annual Review of Biophysics

SN - 1936-122X

ER -