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Kautzmann, Robert; Zoberst, Werner

doi:10.1007/978-3-662-34537-5_15

Cited by 3 publications

(3 citation statements)

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“…The procedure we adopted is as follows: (1) From the experiment data in the large Q range and the known surfactant tail length, we can determine a , b, and an approximate N . (2) We then fix a , b, and N to fit the data in the entire Q range using two other parameters, D and 6. According to the result obtained, we modify a, b, and N slightly, if necessary, to make the fit better.…”

Section: Discussionmentioning

confidence: 99%

Small‐angle neutron scattering study of the structure of protein / detergent complexes

et al. 1990

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Small-angle neutron scattering (SANS) was used to study the structure of protein/sodium dodecylsulfate complexes. Two water soluble proteins, bovine serum albumin (BSA) and ovalbumin (OVA), were used. The protein concentration was kept constant at 1 wt %, and protein/detergent wt ratio varied between 1/1, 1/1.5, 1/2 and 1/3. Absolute intensities of SANS distributions were analyzed by a fractal model. Analyses of large Q portions of SANS distributions established that sodium dodecylsulfate (SDS) molecules bound to a protein/SDS complex form micelle-like clusters. On the other hand, analyses of small Q portions of SANS distributions clearly showed that the arrangement of micelle-like clusters resembles a fractal packing of spheres. We showed that a protein/SDS complex can be characterized by four parameters extracted from the scattering experiment, namely, the average micelle size and its aggregation number, the fractal dimension characterizing the conformation of the micellar chains, the correlation length giving the extent of the unfolded polypeptide chains, and the numbers of micelle-like clusters in the complex.

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Section: Discussionmentioning

confidence: 99%

Small‐angle neutron scattering study of the structure of protein / detergent complexes

et al. 1990

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“…Eqs (1). and(2) it follows that Ew( V ) = Eo( q ' 2 -2 q 6 ) van der Waals energy and the core volume corresponding to this minimum.The values vo and I?, can be easily estimated because a native protein is as tightly packed as a molecular ~rystal.…”

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confidence: 90%

Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first‐order phase transition

1989

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A theory of equilibrium denaturation of proteins is suggested. According to this theory, a cornerstone of protein denaturation is disruption of tight packing of side chains in protein core. Investigation of this disruption is the object of this paper. It is shown that this disruption is an "all-or-none" transition (independent of how compact is the denatured state of a protein and independent of the protein-solvent interactions) because expansion of a globule must exceed some threshold to release rotational isomerization of side chains. Smaller expansion cannot produce entropy compensation of nonbonded energy loss; this is the origin of a free-energy barrier (transition state) between the native and denatured states. The density of the transition state is so high that the solvent cannot penetrate into protein in this state. The results obtained in this paper make it possible to present in the following paper a general phase diagram of protein molecule in solution.

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“…The uses of electrophoresis for separating polysaccharides (257), amino acids and peptides (215), cells (1472), nitrogenous components of molasses and yeast cultures (1103), and isotopes (735, 2049) have been surveyed.…”

Section: Books and Reviewsmentioning

confidence: 99%

Electrophoresis

Strickland¹

1966

Anal. Chem.

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Cited by 3 publications

References 3 publications

Small‐angle neutron scattering study of the structure of protein / detergent complexes

Small‐angle neutron scattering study of the structure of protein / detergent complexes

Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first‐order phase transition

Electrophoresis

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