Concluding Remarks

Several aspects have been mentioned in the previous paragraphs of how reconstitution of Chl a/b-protein complexes can be

Figure 2. Sucrose gradient fractionation of reconstitution mixtures containing the two apoproteins of LHCI-730. FP, free pigments; m-LHCI, monomeric LHCI; d-LHCI, dimer-ic LHCI (LHCI-730).

used as a fine and sophisticated surgical tool in functional analyses of these complexes. Single Chl-binding amino acids, for instance, may be exchanged simply by mutating the bacterially expressed apopro-tein (83). If the corresponding Chl then is lacking in the reconstituted complex, its individual spectroscopic properties may be deduced from spectral differences between this and the native complex.

It should, however, be kept in mind that reconstitution itself is quite a striking example of self-organization of a biological structure. A cue as simple as the mixing of 2 different detergents is sufficient to initiate the correct folding of a medium-size membrane protein and the binding of up to 15 or so pigment molecules of several different kinds to their correct binding sites. The effort seems worthwhile to try and understand this self-organization process itself: what is the sequence of events between the prereconstitution mixture of components and the fully formed stable complex, what are the structural features involved, and which is the driving force? Once we know the answer to these questions, we may understand why Chl ^/¿-protein complexes appear to reconstitute more easily than other pigment-protein complexes. We may then learn to design biomimetic structures that autonomously form in vitro.

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