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Studying excited states of proteins by NMR spectroscopy

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Studying excited states of proteins by NMR spectroscopy. / Mulder, F A; Mittermaier, A; Hon, B et al.

In: Nature Structural and Molecular Biology, Vol. 8, No. 11, 11.2001, p. 932-935.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Mulder, FA, Mittermaier, A, Hon, B, Dahlquist, FW & Kay, LE 2001, 'Studying excited states of proteins by NMR spectroscopy', Nature Structural and Molecular Biology, vol. 8, no. 11, pp. 932-935. https://doi.org/10.1038/nsb1101-932

APA

Mulder, F. A., Mittermaier, A., Hon, B., Dahlquist, F. W., & Kay, L. E. (2001). Studying excited states of proteins by NMR spectroscopy. Nature Structural and Molecular Biology, 8(11), 932-935. https://doi.org/10.1038/nsb1101-932

CBE

Mulder FA, Mittermaier A, Hon B, Dahlquist FW, Kay LE. 2001. Studying excited states of proteins by NMR spectroscopy. Nature Structural and Molecular Biology. 8(11):932-935. https://doi.org/10.1038/nsb1101-932

MLA

Mulder, F A et al. "Studying excited states of proteins by NMR spectroscopy". Nature Structural and Molecular Biology. 2001, 8(11). 932-935. https://doi.org/10.1038/nsb1101-932

Vancouver

Mulder FA, Mittermaier A, Hon B, Dahlquist FW, Kay LE. Studying excited states of proteins by NMR spectroscopy. Nature Structural and Molecular Biology. 2001 Nov;8(11):932-935. https://doi.org/10.1038/nsb1101-932

Author

Mulder, F A ; Mittermaier, A ; Hon, B et al. / Studying excited states of proteins by NMR spectroscopy. In: Nature Structural and Molecular Biology. 2001 ; Vol. 8, No. 11. pp. 932-935.

Bibtex

@article{57913c7f8e864725a6676a90ff98b03f,
title = "Studying excited states of proteins by NMR spectroscopy",
abstract = "Protein structure is inherently dynamic, with function often predicated on excursions from low to higher energy conformations. For example, X-ray studies of a cavity mutant of T4 lysozyme, L99A, show that the cavity is sterically inaccessible to ligand, yet the protein is able to bind substituted benzenes rapidly. We have used novel relaxation dispersion NMR techniques to kinetically and thermodynamically characterize a transition between a highly populated (97%, 25 degrees C) ground state conformation and an excited state that is 2.0 kcal mol(-1) higher in free energy. A temperature-dependent study of the rates of interconversion between ground and excited states allows the separation of the free energy change into enthalpic (Delta H = 7.1 kcal mol(-1)) and entropic (T Delta S = 5.1 kcal mol(-1), 25 degrees C) components. The residues involved cluster about the cavity, providing evidence that the excited state facilitates ligand entry.",
keywords = "Amino Acid Substitution, Bacteriophage T4, Binding Sites, Entropy, Kinetics, Ligands, Magnetic Resonance Spectroscopy, Models, Molecular, Motion, Muramidase, Protein Structure, Secondary, Temperature",
author = "Mulder, {F A} and A Mittermaier and B Hon and Dahlquist, {F W} and Kay, {L E}",
year = "2001",
month = nov,
doi = "10.1038/nsb1101-932",
language = "English",
volume = "8",
pages = "932--935",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Nature Publishing Group",
number = "11",

}

RIS

TY - JOUR

T1 - Studying excited states of proteins by NMR spectroscopy

AU - Mulder, F A

AU - Mittermaier, A

AU - Hon, B

AU - Dahlquist, F W

AU - Kay, L E

PY - 2001/11

Y1 - 2001/11

N2 - Protein structure is inherently dynamic, with function often predicated on excursions from low to higher energy conformations. For example, X-ray studies of a cavity mutant of T4 lysozyme, L99A, show that the cavity is sterically inaccessible to ligand, yet the protein is able to bind substituted benzenes rapidly. We have used novel relaxation dispersion NMR techniques to kinetically and thermodynamically characterize a transition between a highly populated (97%, 25 degrees C) ground state conformation and an excited state that is 2.0 kcal mol(-1) higher in free energy. A temperature-dependent study of the rates of interconversion between ground and excited states allows the separation of the free energy change into enthalpic (Delta H = 7.1 kcal mol(-1)) and entropic (T Delta S = 5.1 kcal mol(-1), 25 degrees C) components. The residues involved cluster about the cavity, providing evidence that the excited state facilitates ligand entry.

AB - Protein structure is inherently dynamic, with function often predicated on excursions from low to higher energy conformations. For example, X-ray studies of a cavity mutant of T4 lysozyme, L99A, show that the cavity is sterically inaccessible to ligand, yet the protein is able to bind substituted benzenes rapidly. We have used novel relaxation dispersion NMR techniques to kinetically and thermodynamically characterize a transition between a highly populated (97%, 25 degrees C) ground state conformation and an excited state that is 2.0 kcal mol(-1) higher in free energy. A temperature-dependent study of the rates of interconversion between ground and excited states allows the separation of the free energy change into enthalpic (Delta H = 7.1 kcal mol(-1)) and entropic (T Delta S = 5.1 kcal mol(-1), 25 degrees C) components. The residues involved cluster about the cavity, providing evidence that the excited state facilitates ligand entry.

KW - Amino Acid Substitution

KW - Bacteriophage T4

KW - Binding Sites

KW - Entropy

KW - Kinetics

KW - Ligands

KW - Magnetic Resonance Spectroscopy

KW - Models, Molecular

KW - Motion

KW - Muramidase

KW - Protein Structure, Secondary

KW - Temperature

U2 - 10.1038/nsb1101-932

DO - 10.1038/nsb1101-932

M3 - Journal article

C2 - 11685237

VL - 8

SP - 932

EP - 935

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 11

ER -