New PDF release: All About Albumin: Biochemistry, Genetics, and Medical

By Theodore Peters Jr.

ISBN-10: 0125521103

ISBN-13: 9780125521109

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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Extra resources for All About Albumin: Biochemistry, Genetics, and Medical Applications

Sample text

Anderson and Weber (1969), using a different approach, polarization of fluorescence of the ligand, 1-anilino-8-naphthosulfonate (ANS), likewise suggested that albumin consists of three segments separated by clefts that provide orientation of the ligand. Foster (1960) explained the expansion of the molecule with increasing acidity with his "club sandwich" model--four stacked subunits that dissociate first to two pairs then to four individual plates still linked by a peptide strand. This model fit well with the limited cleavages by pepsin (Section I,D) and subtilisin (Pederson and Foster, 1969), but needed modification when the triplet domain homology was revealed.

The C-2 H of His-3, which II. Tertiary Structure and Physical Chemical Behavior 45 creates a copper-binding site (Chapter 3, Section II,A,1), was readily identified, as well as that of His-464. His-464 can be seen to lie just outside of a helical stretch, helix h5 of domain III. Other resonances could be assigned to particular fragments, but we see that only two of the resonances of the 17 histidines of HSA have as yet been identified. NMR has also helped to locate ligand sites (Chapter 3) and histidine residues involved in the N --~ B isomerization (Section II,C,l,c).

6. Flexibility The albumin molecule is not in a static, "platonic" state, but has been described by Weber (1975) as flexible and rapidly changing in shape, a "kicking and screaming, stochastic" molecule: The whole molecule tumbles in about 40 nsec (rotational diffusion coefficient). Its loop-link structure permits rapid expansion, contraction, and flexion, some of it intrinsic, some of it related to binding of ligands. 3 s. Choi et al. in 1990 applied the technique of 38 2. Albumin Molecule: Structure and Chemistry ultrasonic spectroscopy and found that expansion and helix-coil transitions relate to pressure wave absorptions at 200 kHz, corresponding to times of 5 lasec for these transformations.

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All About Albumin: Biochemistry, Genetics, and Medical Applications by Theodore Peters Jr.


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