By Theodore Peters Jr.
The 1st of its variety, All approximately Albumin summarizes the chemistry, genetics, metabolism, scientific implications, and advertisement elements of albumin. It presents the main updated sequences, constructions, and compositions of many species, and contains greater than 2000 references.
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Additional info for All About Albumin: Biochemistry, Genetics, and Medical Applications
2-9 is confusing to those of us accustomed to the symmetric linear model of Figs. 2-1 and 2-2, but the relationship between the two models may be more easily understood with the help of Fig. 2-10. tion (Fig. 210B), loops 3, 4, 5, and 9 are seen to be inverted, and loops 3, 6, and 9 are displaced out of the linear pattern. 4. Tertiary Structure in More Detail Albumin has long been recognized to be a highly helical molecule, and the X-ray diffraction results show 67% of the residues of crystalline HSA to be involved in a total of 28 s-helical regions.
Tertiary Structure and Physical Chemical Behavior 31 for both AFP and HSA from their calculations of ~ turns in the predicted secondary structure. , 1983), compared to 19 A by X-ray. , 1983); Hagag et al. ~. 2 ,~ from Tyr-411" X-ray diffraction found a greater distance, ~36 ]k, which He and Carter (1992) conjectured may be due to experimental error and lack of knowledge about the orientation of the fluorescent probe on Tyr-411 and the quencher on Cys-34. Unfortunately, the atomic coordinates of the He and Carter model have not been made public, so that the scientific community cannot make its own distance computations or other assessments.
The apparent constraint of the residue may indeed arise from the nearby tyrosyl groups, which are more numerous in BSA than in HSA. c. Phosphorescence and Optically Detected Magnetic" Resonance. Optically detected magnetic resonance (ODMR) was apparently first applied to albumin in 1982 (Bell and Brenner, 1982). In this procedure the excited triplet state of tryptophan, as a chromophore, is used as a spin probe; its magnetic resonance transitions are detected by optical methods. The phosphorescence at 77 ~ ODMR line width, and zero-field splitting frequency all indicate that the single tryptophan of HSA is buried in a hydrophobic environment, in essential agreement with the fluorescence studies.