Quantitative description of the absorption spectra of the coenzyme in glycogen phosphorylases based on log-normal distribution curves

The absorption spectra of the coenzyme [pyridoxal 5′-phosphate (PLP)] in glycogen phosphorylase a (GPha), glycogen phosphorylase b (GPhb) and of the latter bound to various effectors and substrates were analysed on the basis of log-normal distribution curves. The results obtained showed that the ionization state of the PLP and GPha environment differs from that of GPhb. This divergence was interpreted in terms of tautomeric equilibria between some forms of the Schiff base of PLP and enzymic Lys-679. The ionic forms are slightly more predominant in GPha than they are in GPhb, so ionic and/or hydrogen-bonding interactions between the aromatic ring of PLP and GPha must be stronger than with GPhb. This confirms the purely structural role of the aromatic ring of the coenzyme. Binding of GPhb to AMP and Mg2+ results in the coenzyme adopting a similar state as in GPha. On the other hand, binding to IMP gives rise to no detectable changes in the tautomeric equilibrium of the coenzyme.

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Ultraviolet Absorption Spectra and Dissociation Constants of Diamino-1,3,5-triazines

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc20020429 ◽

2002 ◽

Vol 67 (4) ◽

pp. 429-438 ◽

Cited By ~ 7

Author(s):

Rafael Pérez ◽

Rafael Marín Galvín ◽

José M. Rodríguez Mellado

Keyword(s):

Normal Distribution ◽

Absorption Spectra ◽

Dissociation Constants ◽

Ultraviolet Absorption ◽

Amino Groups ◽

Individual Bands ◽

Ring Nitrogen ◽

Log Normal ◽

The Individual ◽

Log Normal Distribution

This paper presents ultraviolet absorption spectra of two diamino-1,3,5-triazines, namely 1,3,5-triazine-2,4-diamine (DT) and 6-chloro-1,3,5-triazine-2,4-diamine (ClDT). The spectra were fitted to the log-normal distribution. In the more energetic zone of the spectrum both compounds presented common bands, placed around 204-205 and 223-226 nm (depending on the pH of the medium). At higher wavelengths the spectra were different, with bands appearing in the range 235-267 nm. From variations of the maximum absorbances of the individual bands, the pKb values 3.5 ± 0.2 and 1.2 ± 0.1 were obtained for protonation of the ring nitrogen placed between the amine radicals of DT and ClDT, respectively, and 9.35 ± 0.2 and 11.5 ± 0.1 for dissociation of the amino groups of DT and ClDT, respectively.

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A Universal Model for the Log-Normal Distribution of Elasticity in Polymeric Gels and Its Relevance to Mechanical Signature of Biological Tissues

Biology ◽

10.3390/biology10010064 ◽

2021 ◽

Vol 10 (1) ◽

pp. 64

Author(s):

Arnaud Millet

Keyword(s):

Elastic Modulus ◽

Normal Distribution ◽

Biological Tissues ◽

Force Microscopy ◽

Polymeric Gels ◽

Atomic Force ◽

Clear Explanation ◽

Log Normal ◽

Log Normal Distribution

The mechanosensitivity of cells has recently been identified as a process that could greatly influence a cell’s fate. To understand the interaction between cells and their surrounding extracellular matrix, the characterization of the mechanical properties of natural polymeric gels is needed. Atomic force microscopy (AFM) is one of the leading tools used to characterize mechanically biological tissues. It appears that the elasticity (elastic modulus) values obtained by AFM presents a log-normal distribution. Despite its ubiquity, the log-normal distribution concerning the elastic modulus of biological tissues does not have a clear explanation. In this paper, we propose a physical mechanism based on the weak universality of critical exponents in the percolation process leading to gelation. Following this, we discuss the relevance of this model for mechanical signatures of biological tissues.

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