Structural Changes Upon Binding

Changes in C-C distances upon binding of ethylene to an electron-poor R(ll) and electron-rich R(0) center. 

The change in hybridization of the carbons of the olefin toward sp upon coordination to a transition metal relieves strain in strained olefins. Thus, strained olefins bind more strongly than unstrained olefins if the steric and electronic properties of substituents are similar. This effect is illustrated by the displacement of cis-cyclooctene by frons-cyclooctene (Equation 2.12).2  

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The influence of the effectors pyruvamide and phosphate on the quarternary structure of PDCS.c. has been demonstrated by X-ray solution scattering [113]. Whereas phosphate stabilizes the tetrameric structure, the addition of pyruvamide gave rise to a less compact tetramer, due to structural changes upon binding to the regulatory site (for a more detailed description of the substrate activation behaviour see Sects. 4.2 and 6.1). 

SjogrenT, Svensson-Ek M, Hajdu J, Brzezinski P. Proton-couple structural changes upon binding of carbon monoxide to cytochrome cdl A combined flash photolysis and X-ray crystallography study. Biochemistry 2000 39 10967-74. 

Sjoergen, T., Svenson-Ek, M., Hajdu, I., and Brzezinski, P. (2000) Proton-coupling structural change upon binding of carbon monoxide to cytochrome cdi a combine flash... 

H-bonding. Therefore, it can be viewed as a starting point for the creation of loops that undertake relevant structural changes upon binding to an external partner (solvent, another peptide, etc.). This is, after all, an important feature of loops in proteins [82]. 

Cusack, S., Yaremchuk, A., and Tukalo, M. (1996). The crystal structures of T. thermophilus lysyl-tRNA synthetase complexed with E. coli tRNA(Lys) and a T. thermophilus tRNA (Lys) transcript anticodon recognition and conformational changes upon binding of a lysyl-adenylate analogue. EM BO J. 15, 6321—6334. 

Fig. 5. Stereo view showing the substrate access channel in eNOS. The heme is lightly shaded and the substrate, L-Arg, is darkly shaded. The channel is deep yet solvent accessible for ready entry of substrate and exit of product. Part of the access channel is shaped by the second molecule (shaded) in the dimer. There appears to be no requirement for major structural changes upon substrate binding or release.

How does the protein morphology or secondary structure change upon metal binding ... 

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