Human serum albumin structure

The resolution of these columns for protein mixtures, however, was comparably poor. The peak capacity for human serum albumin was near 3 during 20 min gradient elution. Improvement has been reached by covalent binding of PEI (M = 400-600) onto a 330 A silica of 5 pm particle size [38], The peak capacities of ovalbumin and 2a -arid glycoprotein were 30-40 (tgradienl = 20 min). Enhanced peak capacity and resolution probably were due to the more diffuse structure of PEI coupled to silane moieties than that of strictly adsorbed on silica and cross-linked (see Sect, 2.2). Other applications of covalently adsorbed PEI are discussed in Sect. 4.1. 

Solubilization of biomolecules could induce change in the microemulsion structure. For example, in the presence of the human serum albumin and at low R value, the ternary microemulsion AOT/water/isoctane shows a transition to a bicontinuous microstructure [172],... 

Fig. 4. Backscattered Raman and ROA spectra of the n-helical protein human serum albumin in H20 (top pair) and the /3-sheet protein jack bean concanavalin A in acetate buffer solution at pH 5.4, together with MOLSCRIPT diagrams (Kraulis, 1991) of their X-ray crystal structures (PDB codes lao6 and 2cna). 

According to the PDB X-ray crystal structure 1 ao6, human serum albumin contains 69.2% o -helix and 1.7% 3io-helix, the rest being made up of turns and long loops. The amide I ROA couplet centered at 1650 cm-1 (Fig. 4), which is negative at low wavenumber and positive at high,... 

Curry, S., Mandelkow, H., Brick, P. and Franks, N. (1998) Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nature Structural Biology 5, 827-835. 

He, X.M. and Carter, D.C. (1992) Atomic structure and chemistry of human serum albumin. Nature 358, 209-215. 

The nature of the antigenic determinant has been characterized in a male worker with occupational asthma from nickel [415, 416] the antibody recognized Ni2+ bound at the natural Cu2 + /Ni2+ transport site of human albumin. The interpretation was deduced from metal ion blocking experiments and from the good agreement obtained between the pH dependency of the formation of the Ni2 + -albumin complex and the antigen-antibody complex. It was suggested that the antibody interaction depended on a special structural feature of the interaction of Ni2 + with human serum albumin, and perhaps the ability to form an octahedral complex affords one explanation [417]. 

Since the rate constants of bimolecular diffusion-limited reactions in isotropic solution are proportional to T/ these data testify to the fact that the kt values are linearly dependent on the diffusion coefficient D in water, irrespective of whether the fluorophores are present on the surface of the macromolecule (human serum albumin, cobra neurotoxins, proteins A and B of the neurotoxic complex of venom) or are localized within the protein matrix (ribonuclease C2, azurin, L-asparaginase).1 36 1 The linear dependence of the functions l/Q and l/xF on x/t] indicates that the mobility of protein structures is correlated with the motions of solvent molecules, and this correlation results in similar mechanisms of quenching for both surface and interior sites of the macromolecule. 

Fig. 3.17. The crystal structure of human serum albumin (HSA) complexed with four molecules ofmyristic acid (from lbj5.pdb [121][122]). The picture shows the domains (I—III) and subdomains (A and B) of HSA. The primary hydrolytic site is located in subdomain IIIA, and two others probably in subdomain IIA. 

I. Petitpas, T. Grime, A. A. Bhattacharya, S. Curry, Crystal Structures of Human Serum Albumin Complexed with Monounsaturated and Polyunsaturated Fatty Acids , J. Mol. Biol. 2001, 314, 955-960. 

This section will provide an overview on ADME models from our group to illustrate our approach for building predictive models on structurally diverse training sets. Datasets for intestinal human absorption and human serum albumin binding are discussed, while models for other relevant ADME properties have also been obtained. Those models, however, do not stand alone but are used in combination with those models tailored for affinity and selectivity in the frame of multidimensional lead optimization. 

Twine, S., East, M., and Curry, S. Crystal structure analysis of warfarin binding to human serum albumin. Anatomy of dmg site I. /. Biol. Chem. 

Figure 7. Structure and location of the six regions of bovine serum albumin (BSA) and of human serum albumin (HSA) that we have shown to carry antigenic sites. It Is not Implied that the antigenic sites comprise the entire size of the regions shown, but rather that they fall within these regions. Reproduced with permission from Refs. 9, 10, and 11.

In addition to the application of roughened Ag electrodes in SERS measurements, one should add that Geddes et al. [15] have described the use of such Ag electrodes in metal-enhanced fluorescence studies also. The constant current flowing between two silver electrodes in pure water facilitated the growth of fractal-like structures on the cathode. The electrode was coated with a monolayer of human serum albumin protein labeled with Indocyanine Green. It was observed that the fluorescence intensity on the roughened electrode increased approximately the 50-fold, compared to the unroughened electrode. 

FIGURE 4-15 Globul ar protein structures are compact and varied. Human serum albumin (Mr 64,500) has 585 residues in a single chain. Given here are the approximate dimensions its single polypeptide chain would have if it occurred entirely in extended /3 conformation or as an a helix. Also shown is the size of the protein in its native globular form, as determined by X-ray crystallography the polypeptide chain must be very compactly folded to fit into these dimensions. 

Fig. 18 Chemical structure of tetrabromophenol blue and the color change after the reaction with human serum albumin (HSA)...

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