Protein Dynamics, Function and Design
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BeschreibungThis book offers a survey of the current state of research worldwide on the interactions and dynamics of large bilogical molecules such as DNA and proteins and on the effects of dynamics upon structure determination. Authors from renowned laboratories and institutions discuss new findings and new directions for the greater understanding of the interactions of molecules to create life-processes. Although the topics covered in the book require a relatively advanced understanding of current biomedical/biochemical and biophysical science, the overall range of expertise and focus provides a broad survey of experimental techniques and approaches to the problem of understanding molecular recognition and interaction and the potential for drug design and development.
InhaltsverzeichnisDetermining Structures of Protein/DNA Complexes by NMR;
A.M. Gronenborn, G.M. Clore. Fitting Protein Structures to Experimental Data: Lessons from before Your Mother Was Born;
J.C. Hoch, et al. Multisubunit Allosteric Proteins;
W.N. Lipscomb. Studying Protein Structure and Function by Directed Evolution: Examples with Engineered Antibodies;
A. Plückthun. High Pressure Effects on Protein Structure;
K.E. Prehoda, et al. The Role of Molecular Recognition in Activation and Regulation in the Growth Hormone-Prolactin Family of Hormones and Receptors;
A.A. Kossiakoff, et al. Protein Dynamics and Function;
H. Frauenfelder. What Can NMR Tell Us about Protein Motions? A. Jardetzky. The Investigation of Protein Dynamics via the Spectral Density Function;
R.A. Atkinson, J.-F. Lefèvre. NMR Studies of Protein Sidechain Dynamics: Examples from Antifreeze and Calcium-Regulatory Proteins;
L. Spyracopoulos, et al. Monitoring Protein Folding Using Time-Resolved Biophysical Techniques;
K.W. Plaxco, C.M. Dobson. NMR Structure Determination of an Antibiotic-RNA Complex;
S. Yoshizawa, J.D. Puglisi. Index.
Untertitel: Sprache: Englisch.
Verlag: SPRINGER VERLAG GMBH
Erscheinungsdatum: Januar 1999
Seitenanzahl: 222 Seiten