Distance dependence of interactions between charged centres in proteins with common structural features.
Data collected for interactions among redox centres, and interactions between redox centres and acid-base residues in a family of small multihaem cytochromes are analysed. The distance dependent attenuation of the interactions between non-surface charges, for separations that range from 8 to 23 angstroms, can be described by a simple function derived from the Debye-Huckel formalism, fit to 9.5 and 7.6 as values for the relative dielectric constant and Debye length, respectively. However, there is considerable scatter in the data despite the structural similarities among the proteins, which is discussed in the framework of using such simple models in predicting properties of novel proteins.
Instituto de Tecnologia Quìmica e Biológica da Universidade Nova de Lisboa, Rua da Quínta Grande 6, Apt 127, 2780-156 Oeiras, Portugal. louro@itqb.unl.pt
Ricardo O
RO
Louro
Teresa
T
Catarino
Catarina M
CM
Paquete
David L
DL
Turner
D024342:Amino Acids, Acidic / Q000378:metabolism; D024361:Amino Acids, Basic / Q000378:metabolism; D003580:Cytochromes / Q000737:chemistry; D008956:Models, Chemical; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D011506:Proteins / Q000737:chemistry*; D013057:Spectrum Analysis; D055672:Static Electricity; D013329:Structure-Activity Relationship
D024342:Amino Acids, Acidic; D024361:Amino Acids, Basic; D003580:Cytochromes; D011506:Proteins