Referências

References

AKAIKE, H. A new look at the statistical model identification. IEEE transactions on automatic control, [s. l.], vol. 19, no. 6, p. 716–723, 1974.

ALBERTY, R. A. Calculation of biochemical net reactions and pathways by using matrix operations. Biophysical journal, [s. l.], vol. 71, no. 1, p. 507–515, 1996.

ALBERTY, R. A. Chemical equations are actually matrix equations. Journal of chemical education, [s. l.], vol. 68, no. 12, p. 984, 1991.

BHATTI, H. N. et al. Effect of aniline coupling on kinetic and thermodynamic properties of fusarium solani glucoamylase. Applied microbiology and biotechnology, [s. l.], vol. 73, no. 6, p. 1290–1298, 2007.

BLOOMFIELD, V. Computer simulation and data analysis in molecular biology and biophysics: An introduction using r. [S. l.]: Springer Science & Business Media, 2009.

COOPER, A. Thermodynamics and interactions. In: BIOPHYSICAL CHEMISTRY. [S. l.: s. n.], 2004. p. 99–122.

CREIGHTON, T. E. et al. Biophysical chemistry of nucleic acids & proteins. [S. l.]: Distributed by Gardners Books, 2010.

DAHLQUIST, F. [13] the meaning of scatchard and hill plots. Methods in enzymology, [s. l.], vol. 48, p. 270–299, 1978.

DELEAN, A.; MUNSON, P.; RODBARD, D. Simultaneous analysis of families of sigmoidal curves: Application to bioassay, radioligand assay, and physiological dose-response curves. American Journal of Physiology-Endocrinology And Metabolism, [s. l.], vol. 235, no. 2, p. E97, 1978.

DUFF, D.; GILES, C. Spectrophotometric determination of the critical micelle concentration of surfactants. Journal of Colloid and Interface Science, [s. l.], vol. 41, no. 3, p. 407–414, 1972.

EDELHOCH, H.; OSBORNE JR, J. C. The thermodynamic basis of the stability of proteins, nucleic acids, and membranes. Advances in protein chemistry, [s. l.], vol. 30, p. 183–250, 1976.

GANDRUD, C. Reproducible research with r and RStudio. [S. l.]: Chapman; Hall/CRC, 2018.

JOHNSON, K. A. 1 transient-state kinetic analysis of enzyme reaction pathways. In: THE ENZYMES. [S. l.]: Elsevier, 1992. vol. 20, p. 1–61.

KHALIL, M. I. Calculating enthalpy of reaction by a matrix method. Journal of Chemical Education, [s. l.], vol. 77, no. 2, p. 185, 2000.

LAVROVA, A. I. et al. Ordinary differential equations and boolean networks in application to modelling of 6-mercaptopurine metabolism. Royal Society Open Science, [s. l.], vol. 4, no. 4, p. 160872, 2017.

LEONE, F. de A. Fundamentos de cinética enzimática. [S. l.]: Appris Ed., 2021.

LICATA, V. J.; LIU, C.-C. Analysis of free energy versus temperature curves in protein folding and macromolecular interactions. Methods in enzymology, [s. l.], vol. 488, p. 219–238, 2011.

MICHAELIS, L.; MENTEN, M. Die kinetik der invertinwirkung. Biochem Z, [s. l.], vol. 49, no. 4, p. 333–369, 1913.

NETO, B. B.; SCARMINIO, I. S.; BRUNS, R. E. Como fazer experimentos-: Pesquisa e desenvolvimento na ciência e na indústria. [S. l.]: Bookman Editora, 2010.

OSBORNE JR, J. C. et al. The thermodynamics of the self-association of the reduced and carboxymethylated form of apoA-II from the human high density lipoprotein complex. Biochemistry, [s. l.], vol. 15, no. 2, p. 317–320, 1976.

OTAKI, J. M. et al. Availability of short amino acid sequences in proteins. Protein science, [s. l.], vol. 14, no. 3, p. 617–625, 2005.

PARSONS, D.; VALLNER, J. Theoretical models for cooperative binding—i. One-site creator of binding sites. Mathematical Biosciences, [s. l.], vol. 41, no. 3-4, p. 189–215, 1978.

PAULING, L. The oxygen equilibrium of hemoglobin and its structural interpretation. Proceedings of the National Academy of Sciences of the United States of America, [s. l.], vol. 21, no. 4, p. 186, 1935.

PO, H. N.; SENOZAN, N. The henderson-hasselbalch equation: Its history and limitations. Journal of Chemical Education, [s. l.], vol. 78, no. 11, p. 1499, 2001.

ROSS, P. D.; SUBRAMANIAN, S. Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, [s. l.], vol. 20, no. 11, p. 3096–3102, 1981.

SARKAR, D. Lattice: Multivariate data visualization with r. [S. l.]: Springer Science & Business Media, 2008.

SCATCHARD, G. The attractions of proteins for small molecules and ions. Annals of the New York Academy of Sciences, [s. l.], vol. 51, no. 4, p. 660–672, 1949.

SPIESS, A.-N.; NEUMEYER, N. An evaluation of R2 as an inadequate measure for nonlinear models in pharmacological and biochemical research: A monte carlo approach. BMC pharmacology, [s. l.], vol. 10, no. 1, p. 1–11, 2010.

TANG, L. et al. Kinetic mechanism and enantioselectivity of halohydrin dehalogenase from agrobacterium radiobacter. Biochemistry, [s. l.], vol. 42, no. 18, p. 5378–5386, 2003.

TONG, J. et al. QSAR studies of TIBO derivatives as HIV-1 reverse transcriptase inhibitors using HQSAR, CoMFA and CoMSIA. Journal of Molecular Structure, [s. l.], vol. 1168, p. 56–64, 2018.

TRAUT, T. W. Allosteric regulatory enzymes. [S. l.]: Springer Science & Business Media, 2007.

TYUMA, I.; IMAI, K.; SHIMIZU, K. Analysis of oxygen equilibrium of hemoglobin and control mechanism of organic phosphates. Biochemistry, [s. l.], vol. 12, no. 8, p. 1491–1498, 1973.

WAELBROECK, M.; VAN OBBERGHEN, E.; DE MEYTS, P. Thermodynamics of the interaction of insulin with its receptor. Journal of Biological Chemistry, [s. l.], vol. 254, no. 16, p. 7736–7740, 1979.

WICKHAM, H. ggplot2. Wiley interdisciplinary reviews: computational statistics, [s. l.], vol. 3, no. 2, p. 180–185, 2011.

WILKINSON, G. Statistical estimations in enzyme kinetics. Biochemical Journal, [s. l.], vol. 80, no. 2, p. 324–332, 1961.

XIE, Y. Dynamic documents with R and knitr. 2nd. ed. Boca Raton, Florida: Chapman; Hall/CRC, 2015. Available at: http://yihui.org/knitr/.

YUNG-CHI, C.; PRUSOFF, W. H. Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochemical pharmacology, [s. l.], vol. 22, no. 23, p. 3099–3108, 1973.