Molecularly biological matrices

Burridge, K., Path, K., Kelly, T., Nuckolls, G., Turner, C. (1988). Focal adhesions Transmembrane junctions between the extracellular matrix and the cytoskeleton. Ann. Rev. Cell Biol. 4,487-525. Cleveland, D.W. Sullivan, K.F. (1985). Molecular biology and genetics of tubulin. Ann. Rev. Biochem. 54,331-365. 

Laurent, T.C. (1982). In Chemistry and Molecular Biology of the Intercellular Matrix (ed. A. Helfet) p. 703, Academic Press, London. 

The development of soft ionization methods (electrospray ionization and matrix-assisted laser desorption ionization, and others not discussed here) has contributed to the remarkable progress seen in mass spectrometry applied to biochemistry and molecular biology research progress, and is beginning to find applications in archaeology. 

Selectivity is the ability of the bioanalytical method to measure and differentiate the analytes in the presence of components that may be expected to be present. Specificity is the ability to assess unequivocally the analyte in the presence of components that may be expected to be present. In general, analytical methods are selective, and only in same cases also specific (e.g., an LC-MS/MS bioanalytical method is highly selective but not always also specific because it could be possible to find in the complex biological matrix an interference with the same retention time, molecular weight, and main fragment of the analyte of interest). Even if the 2000 Washington conference focuses only on selectivity, it is up to bioanalytical laboratories to differentiate in their documentation between selectivity and specificity or consider them equivalent and use them interchangeably. 

Veis, A., Bhatnagar, R. S. The microfibrillar structure of collagen and the placement of intermolecular covalent crosslinkages. In Chemistry and molecular biology of the intercellular matrix, Vol. 1, pp. 279. Balazs, E. A. (ed.). London, New York Academic Press 1970... 

A review focusing on recent genetic and molecular biological studies of the matrix proteoglycans. The structure-function relationships of some paradigmatic proteoglycans are discussed in depth, and novel aspects of their biology are examined. 

Ninomiya, Y., Castagnola, P., Gerecke, D., Gordon, M. K., andjacenko, O. (1990). The molecular biology of collagens with short triple helical domains. In Extracellular Matrix Genes, (Sandell and Boyd, Eds.). Academic Press, New York. 

Fransson, L.A., "Chemistry and Molecular Biology of the Intercellular Matrix" E.A. Balazs, Ed. 

ReidLM. 1990. Defining hormone and matrix requirements for differentiated epithelia. In Pollard JW, Walker MW, eds. Methods in molecular biology Animal cell culture. Clifton, New Jersey Humana Press, 237-266. 

The biomedical and medical sciences have increasingly demonstrated that human health and disease are strictly related to molecular processes (Engel, 1977). Each change at the molecular or cellular level is reflected in an alteration of a certain compound in a biological matrix such as tissue, serum, or urine (Spiro, 1975). Consequently, the exact quantitative determination of these components is of the highest diagnostic value (Boutwell, 1975). 

In solving problems of enzyme catalysis, molecular biophysics of proteins, biomembranes and molecular biology it is necessary to know the spatial disposition of individual parts. One must also know the depth of immersion of paramagnetic centers in a biological matrix, i.e. the availability of enzyme sites to substrates, distance of electron tunneling between a donor and an acceptor group, position of a spin-label in a membrane and in a protein globule, distribution of the electrostatic field around the PC, etc. 

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