Fibrinolytic action of an enzyme preparation conjugated with specific antibodies

Torchilin, Vladimir P.; Maksimenko, A. V.; Ignashenkova, G. V.; Tishchenko, E. G.; Ermolin, G. A.; Смирнов, В. Н.

doi:10.1007/bf00800017

Cited by 3 publications

(1 citation statement)

References 5 publications

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“…and the tendency towards destabilization caused by the free energy change for unfolding (5)(6)(7)(8)(9)(10)(11). Consequently, the stability of a protein can be increased or decreased by changing amino acids which affect the stabilizing interactions.…”

Section: Introductionmentioning

confidence: 99%

Computational Analysis of the Thermal Stability in Thioredoxins: A Molecular Dynamics Approach

Pedone

Bartolucci

Rossi

1998

Journal of Biomolecular Structure and Dynamics

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The knowledge of the relationship between the three-dimensional structure of a protein and its biological and stability is one of the most challenging problem in protein chemistry, since offers the possibility of changing both the specific action of a protein and its stability. In this work, we have approached the problem with studies on a protein family, the thioredoxins, using homology procedures, molecular dynamics simulations in vacuo at 300 K and 500 K and in water solution at 300 K, to determine the relationship between the three-dimensional structure of these proteins and their thermal stability. A comparative analysis, using computational approach, was performed between two thioredoxins with different resistance to temperature. Results obtained using the molecular dynamics techniques and minimization procedures give explanations of the experimental data, underlining that these techniques are able to correlate the increase in protein stabilization with the conformational and structural changes caused by single amino acid replacement. In addition, we report the factors that can be used as a guide in protein engineering and in site-directed mutagenesis to increase or decrease thermal stabilization for this protein family.

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