| 1. |
- Sedzik, Jan
(författare)
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Fresh water pearls of wisdom on protein crystallization
- 2009
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Ingår i: Molecules. - : World Scientific Publishing Co.. - 9789812832665 ; , s. 331-344
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Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
- When crystallization experiments are undertaken, there is usually not much to do except miserable waiting. In the following, we have compiled some very insightful comments on crystallization.
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| 2. |
- Sedzik, Jan, et al.
(författare)
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Gels mimicking antibodies in their selective recognition of proteins and its potential use for protein crystallization
- 2009
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Ingår i: Molecules: Nucleation, Aggregation and Crystallization: Beyond Medical and Other Implications. - : World Scientific Publishing Co.. - 9789812832665 ; , s. 11-34
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Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
- Using a unique molecular-imprinting method we show in this article that human growth hormone, ribonuclease and myoglobin from horse, lysozyme, hemoglobin and albumin can be adsorbed selectively, indicating that the method may be universal or at least applicable to a great number of proteins. A gel with specific adsorption of three model proteins was synthesized in order to demonstrate that the beds can be employed to remove (traces of) several proteins contaminating a sample (“negative purification”). The degree of selective recognition is high, judging from the fact that myoglobin from horse, but not that from whale, was adsorbed onto a column designed to bind specifically the former protein. This selectivity is noteworthy since these two proteins have similar amino acid sequences and 3-D structures. The method for the synthesis of the specific gels involves polymerization of appropriate monomers (for instance, acrylamide and its derivatives) in the presence of the protein to be adsorbed specifically, granulation of the gel formed, packing a column with the gel particles, washing the column to remove the protein, and finally application of the sample for selective adsorption of the protein present during the polymerization of the monomers. The approach resembles that used for entrapment (immobilization) of proteins for affinity chromatography and somewhat like that for molecular imprinting of small molecules, with the distinct difference that the monomer composition is quite different and thereby the binding mechanism. This mechanism is discussed, for instance, in terms of (i) a new classification system for chromatographic beds based on the number of bonds between the solute and the matrix and the strength of each bond, and (ii) “non-specific bonds” (these bonds are often harmful in conventional chromatography, but we have used them to our advantage). In this classification system, the selective recognition is characterized by a large number of weak bonds. Therefore, so-called functional monomers are not used for the preparation of the gels because they are often charged and, accordingly, give rise to strong electrostatic interactions, i.e. the beds behave to some extent as ion exchangers or matrices for hydrophobic interaction chromatography. In most experiments we have used a polyacrylamide gel with large pores to facilitate diffusion of proteins into and out of the gel granules. When used in chromatography, these soft gels (which can be used repeatedly) allow only rather low flow rates. This problem can be overcome by a new approach to preparing the granules. Potential applications of the selective beds are discussed, as well as future improvements. These beds can be synthesized for selective adsorption also of bio-particles, for instance viruses and bacteria, and in the form of monoliths (continuous beds).
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| 3. |
- Sedzik, Jan, et al.
(författare)
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Imaging of Myelin Membrane Rafts
- 2009
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Ingår i: Journal of Neurochemistry. - : Wiley-Blackwell Publishing Inc.. - 0022-3042 .- 1471-4159. ; 110, s. 126-127
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)
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| 4. |
- Sedzik, Jan
(författare)
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Interactive crystallomic
- 2009
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Ingår i: Molecules: Nucleation, Aggregation and Crystallization: Beyond Medical and Other Implications. - : World Scientific Publishing Co.. - 9789812832665 ; , s. 225-235
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Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
- Biologically important molecules have to be crystallized from solution before their atomic structures can be determined. Once their structures have been determined, reliable and fine structural details, which are crucial for structure-based drug design, can be obtained. Crystallization is an important but very poorly understood process. Our inability to produce good quality crystals is a severe limitation of protein crystallography. In this chapter we present rational guidelines which aim to alter our know-how on crystallization from “black magic” into quantitative and affordable science. We have coined a new word, crystallomic, which can be applied to a diverse range of molecules and may intensify research related to crystallogenesis.
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| 5. |
- Sedzik, Jan, et al.
(författare)
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Molecules : Nucleation, aggregation and crystallization: Beyond medical and other implications
- 2009
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Ingår i: Molecules: Nucleation, Aggregation and Crystallization: Beyond Medical and Other Implications. - : World Scientific Publishing Co.. - 9789812832665 ; , s. 1-352
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Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
- This volume, dealing with Nucleation, Aggregation and Crystallization, consists of a compilation of lectures offered at the international course held at Karolinska Institute and at the scientific meetings of the MARIE Network. The word “nucleation,“ derived from “nuclear family,“ refers to the concept of the progenitor, or the mother and the father of any family. Only in the last few centuries have physicists “borrowed“ the word, and more recently, biologists for Theodor Schwann's cell theory. Most recently, the term has come into use in atomic theory, spectroscopy, and radioactivity, as well as in the fields of atomic bombs, fission, and fusion. Nucleation as a physicochemical process is followed by two poorly understood phenomena aggregation and crystallization which underlie disorders like Alzheimer's and “mad-cow“ disease (aggregation of amyloid plaque), cardiovascular diseases (deposition in coronary vessels of cholesterol and lipids), and the appearance of crystals under physiological conditions (gout, silicoses, and liver or kidney stones). Written by leading scientists in the field, including one Nobel Laureate, this book provides a unique perspective between the physical and chemical sciences on the one hand, and the biological and medical sciences on the other, and should be of considerable value to scientists, physicians, students, and the interested lay public.
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| 6. |
- Sedzik, Jan, et al.
(författare)
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Preface
- 2009
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Ingår i: Molecules. - : WORLD SCIENTIFIC. - 9789812832665 ; , s. v-viii
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Bokkapitel (refereegranskat)
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| 7. |
- Takatsy, Aniko, et al.
(författare)
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Universal method for synthesis of artificial gel antibodies by the imprinting approach combined with a unique electrophoresis technique for detection of minute structural differences of proteins, viruses, and cells (bacteria) : II. Gel antibodies against virus (Semliki Forest Virus)
- 2006
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Ingår i: Journal of Separation Science. - : Wiley. - 1615-9306 .- 1615-9314. ; 29:18, s. 2810-2815
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Tidskriftsartikel (refereegranskat)abstract
- Artificial and highly selective antibodies (in the form of gel granules) against proteins can easily be synthesized by a simple, cost-effective imprinting technique [Liao, J.-L. et al., Chromatographia 1996, 42, 259-262]. Using the same method for synthesis of gel antibodies against viruses in combination with analysis by free zone electrophoresis in a rotating narrow bore tube we have shown that artificial gel antibodies against Semliki Forest Virus (wild type) can sense the difference between this virus and a mutant, although they differ in their chemical composition only by three amino acids in one of the three proteins on the surface of the virus particle. The reason for this extremely high resolution is explained by the fact that we use three types of selectivity: (i) shape selectivity (created by the close fit between the antigen and its imprint in the gel), (ii) bond selectivity in the contact area between the antigen and its imprint in the gel antibody, and (iii) charge selectivity, originating from slightly different structures or/and conformations of the antigens.
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| 8. |
- Yoshimura, T., et al.
(författare)
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ANALYSIS OF N-GLYCANS IN MYELIN
- 2009
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Ingår i: Journal of Neurochemistry. - : WILEY-BLACKWELL PUBLISHING, INC. - 0022-3042 .- 1471-4159. ; 110, s. 112-112
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)
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