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1

Roque, Ana Cecília A., ed. Ligand-Macromolecular Interactions in Drug Discovery. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-244-5.

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2

Woodbury, Charles P. Introduction to macromolecular binding equilibria. CRC Press, 2008.

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3

Ligand-macromolecular interactions in drug discovery: Methods and protocols. Springer, 2009.

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4

Biochemical Pharmacology Symposium (4th 1989 New Haven, Conn.). NMR methods for elucidating macromolecule-ligand interactions: An approach to drug design : proceedings of the Fourth Biochemical Pharmacology Symposium, New Haven, CT, 27-29 July 1989. Edited by Handschumacher Robert E, Armitage Ian M, and Welch Arnold D. Pergamon Press, 1990.

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5

Thermodynamic theory of site-specific binding processes in biological macromolecules. Cambridge University Press, 1995.

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6

Wyman, Jeffries. Binding and linkage: Functional chemistry of biological macromolecules. University Science Books, 1990.

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7

Conley, Edward C. The ion channel factsbook. Academic Press, 1996.

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8

Conley, Edward C. The ion channel factsbook. Academic Press, Harcourt Brace & Co., 1996.

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9

J, Brammar W., ed. The ion channel factsbook. Academic Press, Harcourt Brace & Co., 1996.

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10

Introduction to Macromolecular Binding Equilibria. CRC, 2007.

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11

Sherwood, Dennis, and Paul Dalby. Macromolecular conformations and interactions. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780198782957.003.0025.

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As a polymer of many amino acids, any given protein can, in principle, adopt a huge number of configurations. In reality, however, the biologically stable protein adopts a single configuration that is stable over time. Thermodynamically, this configuration must represent a Gibbs free energy minimum. This chapter therefore explores how the thermodynamics and kinetics of protein folding and unfolding can be investigated experimentally (using, for example, chaotropes, heating or ligand interactions), and how these measurements can be used to enrich our understanding of protein configurations and
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12

Macromolecular Crystallography Deciphering The Structure Function And Dynamics Of Biological Molecules. Springer, 2011.

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13

(Editor), Edward Conley, and William J. Brammar (Editor), eds. Ion Channel Factsbook I: Extracellular Ligand-Gated Channels (Factsbook). Academic Press, 1996.

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14

(Editor), Edward Conley, and William J. Brammar (Editor), eds. Ion Channel Factsbook, Volume 2: Intracellular Ligand-Gated Channels (Factsbook). Academic Press, 1996.

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15

(Editor), Edward Conley, and William J. Brammar (Editor), eds. Ion Channel Factsbook, Volume 2: Intracellular Ligand-Gated Channels (Factsbook). Academic Press, 1996.

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16

Thermodynamic Theory of Site-Specific Binding Processes in Biological Macromolecules. Cambridge University Press, 2005.

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17

Immobilised macromolecules: Application potentials. Springer-Verlag, 1993.

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18

Sleytr, U. B., P. Messner, and D. Pum. Immobilized Macromolecules: Application Potentials (Springer Series in Applied Biology). Springer, 1992.

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19

Handschumacher, R. E. Nmr Methods for Elucidating Macromolecule-Ligand Interactions: An Approach to Drug Design : Proceedings of the Fourth Biochemical Pharmacology Sympos. Pergamon, 1990.

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20

Handschumacher, R. E. Nmr Methods for Elucidating Macromolecule-Ligand Interactions: An Approach to Drug Design : Proceedings of the Fourth Biochemical Pharmacology Sympos. Pergamon, 1990.

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