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Resultat 141-150 av 189

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Numrering	Referens	Omslagsbild	Hitta
141.	Abramsson, ML, et al. (författare) Exploration of lipid-membrane protein interactions a study of an evolutionary deprived in silico designed protein 2023 Ingår i: PROTEIN SCIENCE. - 0961-8368. ; 52:SUPPL 1, s. S115-S115 Konferensbidrag (övrigt vetenskapligt/konstnärligt)
142.	Adam, L, et al. (författare) Specific inhibition of α-synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS 2024 Ingår i: Protein science : a publication of the Protein Society. - 1469-896X. ; 33:8, s. e5091- Tidskriftsartikel (refereegranskat)
143.	Amin, E, et al. (författare) Deciphering the molecular and functional basis of the RhoGAP family proteins: A systematic approach towards selective inactivation of the Rho family proteins 2016 Ingår i: PROTEIN SCIENCE. - 0961-8368. ; 25, s. 128-129 Konferensbidrag (övrigt vetenskapligt/konstnärligt)
144.	Bergdoll, M, et al. (författare) All in the family: Structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly 1998 Ingår i: PROTEIN SCIENCE. - : CAMBRIDGE UNIV PRESS. - 0961-8368. ; 7:8, s. 1661-1670 Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract The crystal structures of three proteins of diverse function and low sequence similarity were analyzed to evaluate structural and evolutionary relationships. The proteins include a bacterial bleomycin resistance protein, a bacterial extradiol dioxygenase,
145.	Berggård, T, et al. (författare) Alpha1-microglobulin chromophores are located to three lysine residues semiburied in the lipocalin pocket and associated with a novel lipophilic compound 1999 Ingår i: Protein Science. - : Wiley. - 0961-8368. ; 8:12, s. 20-2611 Tidskriftsartikel (refereegranskat)abstract Alpha1-microglobulin (alpha1m) is an electrophoretically heterogeneous plasma protein. It belongs to the lipocalin superfamily, a group of proteins with a three-dimensional (3D) structure that forms an internal hydrophobic ligand-binding pocket. Alpha1m carries a covalently linked unidentified chromophore that gives the protein a characteristic brown color and extremely heterogeneous optical properties. Twenty-one different colored tryptic peptides corresponding to residues 88-94, 118-121, and 122-134 of human alpha1m were purified. In these peptides, the side chains of Lys92, Lys118, and Lys130 carried size heterogeneous, covalently attached, unidentified chromophores with molecular masses between 122 and 282 atomic mass units (amu). In addition, a previously unknown uncolored lipophilic 282 amu compound was found strongly, but noncovalently associated with the colored peptides. Uncolored tryptic peptides containing the same Lys residues were also purified. These peptides did not carry any additional mass (i.e., chromophore) suggesting that only a fraction of the Lys92, Lys118, and Lys130 are modified. The results can explain the size, charge, and optical heterogeneity of alpha1m. A 3D model of alpha1m, based on the structure of rat epididymal retinoic acid-binding protein (ERABP), suggests that Lys92, Lys118, and Lys130 are semiburied near the entrance of the lipocalin pocket. This was supported by the fluorescence spectra of alpha1m under native and denatured conditions, which indicated that the chromophores are buried, or semiburied, in the interior of the protein. In human plasma, approximately 50% of alpha1m is complex bound to IgA. Only the free alpha1m carried colored groups, whereas alpha1m linked to IgA was uncolored.
146.	Bernfur, Katja, et al. (författare) The chloroplast-localized small heat shock protein Hsp21 associates with the thylakoid membranes in heat-stressed plants 2017 Ingår i: Protein Science. - : Wiley. - 0961-8368. ; 26:9, s. 1773-1784 Tidskriftsartikel (refereegranskat)abstract The small heat shock protein (sHsp) chaperones are crucial for cell survival and can prevent aggregation of client proteins that partially unfold under destabilizing conditions. Most investigations on the chaperone activity of sHsps are based on a limited set of thermosensitive model substrate client proteins since the endogenous targets are often not known. There is a high diversity among sHsps with a single conserved β-sandwich fold domain defining the family, the α-crystallin domain, whereas the N-terminal and C-terminal regions are highly variable in length and sequence among various sHsps and conserved only within orthologues. The endogenous targets are probably also varying among various sHsps, cellular compartments, cell type and organism. Here we have investigated Hsp21, a non-metazoan sHsp expressed in the chloroplasts in green plants which experience huge environmental fluctuations not least in temperature. We describe how Hsp21 can also interact with the chloroplast thylakoid membranes, both when isolated thylakoid membranes are incubated with Hsp21 protein and when plants are heat-stressed. The amount of Hsp21 associated with the thylakoid membranes was precisely determined by quantitative mass spectrometry after metabolic 15N-isotope labeling of either recombinantly expressed and purified Hsp21 protein or intact Arabidopsis thaliana plants. We found that Hsp21 is among few proteins that become associated with the thylakoid membranes in heat-stressed plants, and that approximately two thirds of the pool of chloroplast Hsp21 is affected. We conclude that for a complete picture of the role of sHsps in plant stress resistance also their association with the membranes should be considered.
147.	Bernsel, Andreas, et al. (författare) Improved membrane protein topology prediction by domain assignments. 2005 Ingår i: Protein Sci. - 0961-8368. ; 14:7, s. 1723-8 Tidskriftsartikel (refereegranskat)
148.	Berthold, Deborah A., et al. (författare) Screening for functional expression and overexpression of a family of diiron-containing interfacial membrane proteins using the univector recombination system 2003 Ingår i: Protein Science. - 0961-8368. ; 12:1, s. 124-134 Tidskriftsartikel (refereegranskat)
149.	Castell, Alina, et al. (författare) Rv0216, a conserved hypothetical protein from Mycobacterium tuberculosis that 2005 Ingår i: Protein Sci. - 0961-8368. ; 14:7, s. 1850-62 Tidskriftsartikel (refereegranskat)
150.	Chen, GF, et al. (författare) Bri2 BRICHOS molecular chaperone activity is decoupled from its ability to inhibit amyloid fibril formation 2017 Ingår i: PROTEIN SCIENCE. - 0961-8368. ; 26, s. 31-32 Konferensbidrag (övrigt vetenskapligt/konstnärligt)

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