Protein–ligand interactions include two components: energetic contributions and shape complementarity.
Keywords: hydrophobic effect; hydrogen bonds; shape complementarity; molecular recognition; receptor–ligand interactions
Protein–Ligand Interactions: Energetic Contributions and Shape Complementarity
Chung‐Jung Tsai, Frederick Cancer Research and Development Center, Frederick, Maryland, USA
Raquel Norel, Tel Aviv University, Tel Aviv, Israel
Haim J Wolfson, Tel Aviv University, Tel Aviv, Israel
Jacob V Maizel, Frederick Cancer Research and Development Center, Frederick, Maryland, USA
Ruth Nussinov, Frederick Cancer Research and Development Center, Frederick, Maryland, USA
Published online: April 2001
DOI: 10.1038/npg.els.0001343
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Figure 1. Examples of protein–protein interfaces. (a) Cytochrome C¢ (PDB code 1bbhAB) displays a strong hydrophobic effect. The two chains are displayed in different colours and the backbones of the amino acids belonging to the interface are shown in darker colours. Only the side-chain of the residues which are actually in contact across the interface as well as on the surface are drawn. The hydrophobic residues are yellow and hydrophilic residues are in cyan.
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Figure 2. Barnase barstar complex (PDB code 1bgsBF) displays a weak hydrophobic effect. The colour scheme is the same as in Figure
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