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 Results for DC.creator="T." AND DC.creator="L." AND DC.creator="Blundell" in section 12.1.3 of volume F
Properties of heavy-atom compounds and their complexes
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3, pp. 318-320 [ doi:10.1107/97809553602060000837 ]
... times more slowly at 4C than at ambient temperature (Blundell, 1968). A lower temperature allows greater control over the ... bind may do so upon elevation of the temperature. References Blundell, T. L. (1968). Unpublished results. Gilliland, G. L., Tung, ...

Solubility of heavy-atom compounds
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.6, pp. 319-320 [ doi:10.1107/97809553602060000837 ]
... scanning transmission electron microscope. Science, 206, 1419-1421. O'Halloran, T. V., Lippard, S. J., Richmond, T. J. & Klug, A. (1987). Multiple heavy-atom reagents for ...

Effect of precipitants and buffers on heavy-atom binding
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.5, p. 319 [ doi:10.1107/97809553602060000837 ]
... complexes formed tend to be relatively unstable. References Gilliland, G. L., Tung, M., Blakeslee, D. M. & Ladner, J. E. (1994). ...

Effect of pH
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.4, pp. 318-319 [ doi:10.1107/97809553602060000837 ]
Effect of pH 12.1.3.4. Effect of pH Although the pKa of an individual amino acid in solution is generally defined within narrow limits, environmental and steric factors give rise to a wide range of values in proteins. Thus, the hydrogen-ion concentration influences the thermodynamic and kinetic stability of potential complexes. ...

Oxidation state of metal ions in protein crystals
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.3, p. 318 [ doi:10.1107/97809553602060000837 ]
Oxidation state of metal ions in protein crystals 12.1.3.3. Oxidation state of metal ions in protein crystals In the environment of a living cell, the following oxidation states tend to be stable: References International Tables for Crystallography (2012). Vol. F, ch. 12.1, p. 318 International Union of Crystallography 2012 | home ...

Lability
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.2, p. 318 [ doi:10.1107/97809553602060000837 ]
Lability 12.1.3.2. Lability The rates at which ligands enter and leave a metal complex are important in the formation of heavy-atom derivatives, especially the covalent complexes of mercury, gold and platinum. The rate-determining step in unimolecular SN1 reactions is the expulsion of the leaving ligand from the metal complexes ...

Stability
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.1, p. 318 [ doi:10.1107/97809553602060000837 ]
Stability 12.1.3.1. Stability Ligands may be classified as either hard or soft. Hard ligands tend to be electronegative and interact electrostatically, with little delocalization of electron density. Water molecules, glutamates, aspartates, terminal carboxylates, and hydroxyl groups of serine and threonine from the protein, as well as acetate and citrate ions from ...

Effect of concentration, time of soak and temperature on heavy-atom binding
Carvin, D., Islam, S. A., Sternberg, M. J. E. and Blundell, T. L.  International Tables for Crystallography (2012). Vol. F, Section 12.1.3.7, p. 320 [ doi:10.1107/97809553602060000837 ]
... times more slowly at 4C than at ambient temperature (Blundell, 1968). A lower temperature allows greater control over the ... bind may do so upon elevation of the temperature. References Blundell, T. L. (1968). Unpublished results. Ringe, D., Petsko, G. ...

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