Effects of structural memory in protein reactions

Barabash, Yu. M.; Berezetskaya, N. M.; Christophorov, L. N.; Goushcha, A. O.; Kharkyanen, V. N.
March 2002
Journal of Chemical Physics;3/8/2002, Vol. 116 Issue 10, p4339
Academic Journal
Specific effects of the coupling of protein reactions to slow protein structure dynamics are studied. We focus on accumulation of structural changes produced in consecutive protein cycles and eventually modifying the cycle itself. We showed previously [Christophorov et al., Chem. Phys. 256, 45 (2000); Goushcha et al., Biophys. J. 79, 1273 (2000)] that such an effective interaction between cycles can cause the thresholdlike emergence of a new stable functional state of the protein macromolecule. To elucidate this mechanism, we have performed numerical modeling of the reaction kinetics in a two-state system coupled to diffusion in the corresponding conformational potentials. Specifically, the model is related to the charge separation and recombination processes in photosynthetic reaction centers (RCs). It is shown that the percentage of RCs remaining structurally deformed after recombination, until the next photoexcitation event (“memory-bearing” centers), can be quite low. Nonetheless, under prolonged photoexcitation it is sufficient for driving eventually all the RCs to a state of high charge-separation efficiency. The dependence of this efficiency on quasistationary photoexcitation intensity is pronouncedly hysteretic. The conformation potentials anharmonicity extends the bistability range noticeably, thereby improving RC adaptation properties. Experimental protocols to detect the memory-bearing centers in the RC ensemble are proposed, simulated and tested, disqualifying the electron escape to hypothetical redox traps. The technique proposed can be used in the studies of cooperative effects under repeated cycling of biomolecules. © 2002 American Institute of Physics.


Related Articles

  • X-ray Studies of Biological Macromolecules at the Shubnikov Institute of Crystallography of the Russian Academy of Sciences. Kuranova, I. P. // Crystallography Reports;Jul2001, Vol. 46 Issue 4, p601 

    The results of X-ray diffraction studies of a number of proteins and the carnation mottle virus performed over a period from 1970 to 2000 at the laboratory created by Academician B.K. Vainshtein at the Shubnikov Institute of Crystallography of the Russian Academy of Sciences are surveyed. The...

  • BEAMS (BEAds Modelling System): a set of computer programs for the generation, the visualization and the computation of the hydrodynamic and conformational properties of bead models of proteins. Spotorno, Bruno; Piccinini, Luca; Tassara, Giovanni; Ruggiero, Carmelina; Nardini, Marco; Molina, Francesco; Rocco, M. // European Biophysics Journal;1997, Vol. 25 Issue 5/6, p373 

    Spheres, cylinders or ellipsoids, whose hydrodynamic properties can be computed from analytical or semi-analytical expressions, have been traditionally used as low-resolution approximate descriptors of macromolecular size and shape. However, these simple geometrical bodies can seldom faithfully...

  • Characterization of Protein and Peptide Stability and Solubility in Non-Aqueous Solvents. Stevenson, Cynthia L. // Current Pharmaceutical Biotechnology;Sep2000, Vol. 1 Issue 2, p165 

    Small molecule parenterals have often been formulated as solutions or suspensions in non-aqueous conditions, however, this technology has not found widespread use in the formulation of macromolecules. Formulation of proteins and peptides has primarily been achieved through aqueous solutions or...

  • Mineralogical signatures of stone formation mechanisms. Gower, Laurie B.; Amos, Fairland F.; Khan, Saeed R. // Urological Research;Aug2010, Vol. 38 Issue 4, p281 

    The mechanisms involved in biomineralization are modulated through interactions with organic matrix. In the case of stone formation, the role of the organic macromolecules in the complex urinary environment is not clear, but the presence of mineralogical �signatures� suggests that some...

  • AAA proteins: in search of a common molecular basis. Maurizi, Michael R.; Chou-Chi H. Li // EMBO Reports;Nov2001, Vol. 2 Issue 11, p980 

    The article presents information on the International Meeting on Cellular Functions of AAA Proteins organized by Koreaki Ito and Teru Ogura, which took place in Kyoto, Japan, from March 13-16, 2001. AAA proteins do a lot of heavy work in the cell, erecting or disassembling complexes, unfolding...

  • VirB8: a conserved type IV secretion system assembly factor and drug target. Baron, Christian // Biochemistry & Cell Biology;Dec2006, Vol. 84 Issue 6, p890 

    Type IV secretion systems are used by many Gram-negative bacteria for the translocation of macromolecules (proteins, DNA, or DNA–protein complexes) across the cell envelope. Among them are many pathogens for which type IV secretion systems are essential virulence factors. Type IV...

  • Short Peptide Segment and Insulin Co-Assembly Forms Cytotoxic Oligomers. Mao, Jie; Chen, Mei-Sha; Chen, Yong-Xiang; Zhao, Yu-Fen; Li, Yan-Mei // International Journal of Peptide Research & Therapeutics;Sep2013, Vol. 19 Issue 3, p185 

    Insulin assembly follows different pathways under different environments. But the mechanism of insulin assembly and the pathology of insulin-related amyloidosis diseases remain unclear. This work, illustrating different pathways of insulin aggregation induced by short peptide segment, may shed...

  • Effective binding force calculation in a dimeric protein by molecular dynamics simulation. Sergi, Alessandro; Ciccotti, Giovanni; Falconi, Mattia; Desideri, Alessandro; Ferrario, Mauro // Journal of Chemical Physics;4/8/2002, Vol. 116 Issue 14, p6329 

    A good example of macromolecular recognition is found in the interaction of the two monomers of the dimeric superoxide dismutase protein found in Photobacterium leiognathi. We have produced, by molecular dynamics simulation techniques, a specific path for the rupture of the dimer and calculated...

  • Research Highlights.  // Nature Biotechnology;Apr2007, Vol. 25 Issue 4, p435 

    The article discusses several studies related to biotechnology. According to a study published in "Science," penicillin-binding proteins may exist in a complex with glycosyltransferases. Meanwhile, a study on the characterization of polyreactive antibodies published in "Cell Host Microbe" is...


Read the Article


Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics