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
SN - 0925-2738
VL - 32
SP - 273
EP - 280
JO - Journal of Biomolecular N M R
JF - Journal of Biomolecular N M R
IS - 4
ER -