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Protein-ligand interactions disadvantages

Competitive desorption (elution) has the advantage of very smooth conditions for protein structure, but the disadvantage of difficult removing of the ligand when further biospecific interactions are intended. [Pg.111]

The advantages of this method are (1) different nanodiscs diameters can be obtained with different MSP sequences (2) the protein is in a bilayer-mimicking environment (3) both the cytoplasmic and the periplasmic exposed regions of the protein are easily accessible with ligands, nucleotides, interacting proteins, etc., without the problems associated with the directional incorporation of the proteins in liposomes and the compartmentalization between lumen and bulk water. The disadvantages are (1) the reconstitution in nanodiscs is protein-specific and requires optimization of the protocol and of the MSP to be used (2) the maximal concentrations achievable are less than 100 pM. [Pg.126]

See other pages where Protein-ligand interactions disadvantages is mentioned: [Pg.187]    [Pg.69]    [Pg.230]    [Pg.183]    [Pg.3]    [Pg.412]    [Pg.141]    [Pg.17]    [Pg.69]    [Pg.128]    [Pg.26]    [Pg.515]    [Pg.4028]    [Pg.232]    [Pg.156]    [Pg.156]    [Pg.173]    [Pg.2087]    [Pg.289]    [Pg.473]    [Pg.185]    [Pg.504]    [Pg.152]    [Pg.85]    [Pg.79]    [Pg.86]    [Pg.412]    [Pg.393]    [Pg.599]    [Pg.1443]    [Pg.197]    [Pg.2078]    [Pg.22]    [Pg.300]    [Pg.553]    [Pg.556]    [Pg.199]    [Pg.102]    [Pg.203]    [Pg.24]    [Pg.35]    [Pg.460]    [Pg.880]    [Pg.262]    [Pg.43]    [Pg.249]    [Pg.49]    [Pg.186]    [Pg.385]   
See also in sourсe #XX -- [ Pg.194 , Pg.195 , Pg.196 , Pg.200 ]



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