@inbook {18698,
	title = {Determining Protein Dynamics from 15N Relaxation Data by Using DYNAMICS},
	booktitle = {Protein NMR Techniques},
	series = {Methods in Molecular Biology},
	volume = {831},
	year = {2012},
	month = {2012///},
	pages = {485 - 511},
	publisher = {Humana Press},
	organization = {Humana Press},
	abstract = {Motions are essential for protein function, and knowledge of protein dynamics is a key to our understanding the mechanisms underlying protein folding and stability, ligand recognition, allostery, and catalysis. In the last two decades, NMR relaxation measurements have become a powerful tool for characterizing backbone and side chain dynamics in complex biological macromolecules such as proteins and nucleic acids. Accurate analysis of the experimental data in terms of motional parameters is an essential prerequisite for developing physical models of motions to paint an adequate picture of protein dynamics. Here, I describe in detail how to use the software package DYNAMICS that was developed for accurate characterization of the overall tumbling and local dynamics in a protein from nuclear spin-relaxation rates measured by NMR. Step-by-step instructions are provided and illustrated through an analysis of 15 N relaxation data for protein G.},
	keywords = {Biomedical and Life Sciences},
	isbn = {978-1-61779-480-3},
	url = {http://www.springerlink.com/content/q667p0k138058103/abstract/},
	author = {Fushman, David},
	editor = {Shekhtman,Alexander and Burz,David S. and Walker,John M.}
}
@inbook {18696,
	title = {Characterization of the Overall Rotational Diffusion of a Protein From 15N Relaxation Measurements and Hydrodynamic Calculations},
	booktitle = {Protein NMR Techniques},
	series = {Methods in Molecular Biology},
	volume = {278},
	year = {2004},
	month = {2004///},
	pages = {139 - 159},
	publisher = {Humana Press},
	organization = {Humana Press},
	abstract = {In this chapter, we discuss experimental and theoretical methods for characterizing the overall rotational diffusion of molecules in solution. The methods are illustrated for the B3 domain of protein G, a small protein with rotational anisotropy of D par / D perp = 1.4. The rotational diffusion tensor of the protein is determined directly from 15 N relaxation measurements. The experimental data are treated assuming various possible models for the overall tumbling: isotropic, axially symmetric, and fully anisotropic, and the results of these analyses are compared to determine an adequate diffusion model for the protein. These experimentally derived characteristics of the protein are compared with the results of theoretical calculations of the diffusion tensor using various hydrodynamic models, to find optimal models and parameter sets for theoretical predictions. We also derive model-free characteristics of internal backbone motions in the protein, to show that different models for the overall motion can result in significantly different pictures of motion. This emphasizes the necessity of accurately characterizing the overall tumbling of a molecule to determine its local dynamics.},
	keywords = {Biomedical and Life Sciences},
	isbn = {978-1-59259-809-0},
	url = {http://www.springerlink.com/content/h6w35487x3q1g6x7/abstract/},
	author = {Blake-Hall,Jennifer and Walker,Olivier and Fushman, David},
	editor = {Downing,A. Kristina and Walker,John M.}
}
@article {18693,
	title = {A comparative study of the backbone dynamics of two closely related lipid binding proteins: Bovine heart fatty acid binding protein and porcine ileal lipid binding protein},
	journal = {Molecular and Cellular Biochemistry},
	volume = {192},
	year = {1999},
	month = {1999///},
	pages = {109 - 121},
	abstract = {The backbone dynamics of bovine heart fatty acid binding protein (H-FABP) and porcine ileal lipid binding protein (ILBP) were studied by 15N NMR relaxation (T1 and T2) and steady state heteronuclear 15N1H NOE measurements. The microdynamic parameters characterizing the backbone mobility were determined using the {\textquoteleft}model-free{\textquoteright} approach. For H-FABP, the non-terminal backbone amide groups display a rather compact protein structure of low flexibility. In contrast, for ILBP an increased number of backbone amide groups display unusually high internal mobility. Furthermore, the data indicate a higher degree of conformational exchange processes in the {\textmu}sec-msec time range for ILBP compared to H-FABP. These results suggest significant differences in the conformational stability for these two structurally highly homologous members of the fatty acid binding protein family.},
	keywords = {Biomedical and Life Sciences},
	isbn = {0300-8177},
	doi = {10.1023/A:1006834708786},
	url = {http://www.springerlink.com/content/w2j255781546j880/abstract/},
	author = {L{\"u}cke,Christian and Fushman, David and Ludwig,Christian and Hamilton,James A. and Sacchettini,James C. and R{\"u}terjans,Heinz}
}
