Dynamical characterization of residual and non-native structures in a partially folded protein by (15)N NMR relaxation using a model based on a distribution of correlation times.
A spectral density model based on a truncated lorentzian distribution of correlation times is used to analyze the nanosecond time-scale dynamics of the partially unfolded domain 2 of annexin I from its (15)N NMR relaxation parameters measured at three magnetic field strengths. The use of a distribution of correlation times enables the characterization of the dynamical features of the NH bonds of the protein in terms of heterogeneity of dynamical states in the nanosecond range. The variation along the sequence of the two dynamical parameters introduced, namely the center and the width of the distribution, points out the different types of residual secondary structures present in the D2 domain. Moreover, it allows a physically sensible interpretation of the dynamical behavior of the different residual helices and of the non-native structures. Also, a striking correspondence is found between the parameters obtained using an extended Lipari and Szabo model and the parameters obtained using the distribution of correlation times. This result led us to propose a specific interpretation of the model-free order parameter for internal motions in the nanosecond range in the case of unfolded states.
Ochsenbein
Françoise
F
CNRS, Institut de Chimie des Substances Naturelles, F-91190 Gif sur Yvette, France. carine@icsn.cnrs-gif.fr
Neumann
Jean-Michel
JM
Guittet
Eric
E
van Heijenoort
Carine
C
D017305:Annexin A1 / Q000737:chemistry*; D008280:Magnetics; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D017711:Nonlinear Dynamics; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding
D017305:Annexin A1; D009587:Nitrogen Isotopes; D010446:Peptide Fragments