Abstract
Protein-protein binding is associated with catalysis, regulation, immune response, and inhibition. The binding of identical subunits forming homodimers is interesting. The folding and binding of homodimers are further intriguing. There are 2-state (2S) and 3-state (3S) homodimer complexes where 3SMI with monomer intermediate and 3SDI with dimer intermediate exit. We describe some of the characteristic features of 2S and 3S homodimer folding and binding in this chapter.
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References
Lulu S, Suresh A, Karthikraja V, Arumugam M, Kayathri R, Kangueane P. Structural features for homodimer folding mechanism. J Mol Graph Model. 2009;28(2):88–94.
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Exercises
Exercises
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1.
Illustrate the three states of homodimer folding.
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2.
Show the distribution of interface area to monomer size for all the three states of homodimers.
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3.
Illustrate a homodimer using an example.
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4.
Illustrate the difference in the three states of homodimers using structures.
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5.
Show the distribution of the ratio of interface to monomer size using a suitable chart.
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6.
Illustrate large, medium, and small homodimer interfaces using diagrams.
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7.
State the experiment used for studying homodimer folding.
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8.
What are the three states of homodimer folding?
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9.
What are the usual molecular functions associated with 2S, 3SMI, and 3SDI homodimers?
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Kangueane, P., Nilofer, C. (2018). Homodimer Protein Folding and Binding. In: Protein-Protein and Domain-Domain Interactions. Springer, Singapore. https://doi.org/10.1007/978-981-10-7347-2_10
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DOI: https://doi.org/10.1007/978-981-10-7347-2_10
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Publisher Name: Springer, Singapore
Print ISBN: 978-981-10-7346-5
Online ISBN: 978-981-10-7347-2
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