Interpreting Dynamically-Averaged Scalar Couplings in Proteins

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Standard

Interpreting Dynamically-Averaged Scalar Couplings in Proteins. / Lindorff-Larsen, Kresten; Best, Robert B.; Vendruscolo, Michele.

I: Journal of Biomolecular NMR, Bind 32, Nr. 4, 2005, s. 273-280.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Lindorff-Larsen, K, Best, RB & Vendruscolo, M 2005, 'Interpreting Dynamically-Averaged Scalar Couplings in Proteins', Journal of Biomolecular NMR, bind 32, nr. 4, s. 273-280. https://doi.org/10.1007/s10858-005-8873-0

APA

Lindorff-Larsen, K., Best, R. B., & Vendruscolo, M. (2005). Interpreting Dynamically-Averaged Scalar Couplings in Proteins. Journal of Biomolecular NMR, 32(4), 273-280. https://doi.org/10.1007/s10858-005-8873-0

Vancouver

Lindorff-Larsen K, Best RB, Vendruscolo M. Interpreting Dynamically-Averaged Scalar Couplings in Proteins. Journal of Biomolecular NMR. 2005;32(4):273-280. https://doi.org/10.1007/s10858-005-8873-0

Author

Lindorff-Larsen, Kresten ; Best, Robert B. ; Vendruscolo, Michele. / Interpreting Dynamically-Averaged Scalar Couplings in Proteins. I: Journal of Biomolecular NMR. 2005 ; Bind 32, Nr. 4. s. 273-280.

Bibtex

@article{d90b377074c211dbbee902004c4f4f50,
title = "Interpreting Dynamically-Averaged Scalar Couplings in Proteins",
abstract = "The experimental determination of scalar three-bond coupling constants represents a powerful method to probe both the structure and dynamics of proteins. The detailed structural interpretation of such coupling constants is usually based on Karplus relationships, which allow the measured couplings to be related to the torsion angles of the molecules. As the measured couplings are sensitive to thermal fluctuations, the parameters in the Karplus relationships are better derived from ensembles representing the distributions of dihedral angles present in solution, rather than from single conformations. We present a method to derive such parameters that uses ensembles of conformations determined through dynamic-ensemble refinement - a method that provides structural ensembles that simultaneously represent both the structure and the associated dynamics of a protein.",
author = "Kresten Lindorff-Larsen and Best, {Robert B.} and Michele Vendruscolo",
note = "Key words protein dynamics - Karplus relationship - protein structure - scalar couplings",
year = "2005",
doi = "10.1007/s10858-005-8873-0",
language = "English",
volume = "32",
pages = "273--280",
journal = "Journal of Biomolecular N M R",
issn = "0925-2738",
publisher = "Springer",
number = "4",

}

RIS

TY - JOUR

T1 - Interpreting Dynamically-Averaged Scalar Couplings in Proteins

AU - Lindorff-Larsen, Kresten

AU - Best, Robert B.

AU - Vendruscolo, Michele

N1 - Key words protein dynamics - Karplus relationship - protein structure - scalar couplings

PY - 2005

Y1 - 2005

N2 - The experimental determination of scalar three-bond coupling constants represents a powerful method to probe both the structure and dynamics of proteins. The detailed structural interpretation of such coupling constants is usually based on Karplus relationships, which allow the measured couplings to be related to the torsion angles of the molecules. As the measured couplings are sensitive to thermal fluctuations, the parameters in the Karplus relationships are better derived from ensembles representing the distributions of dihedral angles present in solution, rather than from single conformations. We present a method to derive such parameters that uses ensembles of conformations determined through dynamic-ensemble refinement - a method that provides structural ensembles that simultaneously represent both the structure and the associated dynamics of a protein.

AB - The experimental determination of scalar three-bond coupling constants represents a powerful method to probe both the structure and dynamics of proteins. The detailed structural interpretation of such coupling constants is usually based on Karplus relationships, which allow the measured couplings to be related to the torsion angles of the molecules. As the measured couplings are sensitive to thermal fluctuations, the parameters in the Karplus relationships are better derived from ensembles representing the distributions of dihedral angles present in solution, rather than from single conformations. We present a method to derive such parameters that uses ensembles of conformations determined through dynamic-ensemble refinement - a method that provides structural ensembles that simultaneously represent both the structure and the associated dynamics of a protein.

U2 - 10.1007/s10858-005-8873-0

DO - 10.1007/s10858-005-8873-0

M3 - Journal article

C2 - 16211481

VL - 32

SP - 273

EP - 280

JO - Journal of Biomolecular N M R

JF - Journal of Biomolecular N M R

SN - 0925-2738

IS - 4

ER -

ID: 83555