Results 1 to 10 of about 490,027 (386)

Preparation of Polyrotaxane Fibers. Part II: Tensile Properties of Polyrotaxane Fibers Treated with Two Cross-linking Reagents [PDF]

open access: green, 2010
Polyrotaxane fibers prepared with wet spinning of polyrotaxane consisting of poly(ethylene glycol) and cyclodextrins were cross-linked with two different cross-linking reagents, i.e., divinyl sulfone (DVS) and ethylene glycol diglycidyl ether (EGDE), to ...
Abe, Koji   +6 more
core   +3 more sources

Ligand-Induced Movements of Inner Transmembrane Helices of Glut1 Revealed by Chemical Cross-Linking of Di-Cysteine Mutants [PDF]

open access: yesPLoS ONE, 2012
The relative orientation and proximity of the pseudo-symmetrical inner transmembrane helical pairs 5/8 and 2/11 of Glut1 were analyzed by chemical cross-linking of di-cysteine mutants.
A Carruthers   +57 more
core   +6 more sources

Investigation of the organization of rhodopsin in the sheep photoreceptor membrane by using cross-linking reagents. [PDF]

open access: greenBiochemical Journal, 1979
The organization of rhodopsin in the photoreceptor membrane of sheep rod outer segments was investigated by using a variety of bifunctional reagents. Of the nine reagents used, seven gave oligomeric opsin species, whereas two, copper phenanthroline and ...
John B. C. Findlay
semanticscholar   +2 more sources

Transmembrane helical interactions in the CFTR channel pore [PDF]

open access: yesPLoS Computational Biology, 2017
Mutations in the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) gene affect CFTR protein biogenesis or its function as a chloride channel, resulting in dysregulation of epithelial fluid transport in the lung, pancreas and other organs in ...
Das, Jhuma   +5 more
core   +4 more sources

Covalent cross‐linking of proteins without chemical reagents [PDF]

open access: greenProtein Science, 2002
AbstractA facile method for the formation of zero‐length covalent cross‐links between protein molecules in the lyophilized state without the use of chemical reagents has been developed. The cross‐linking process is performed by simply sealing lyophilized protein under vacuum in a glass vessel and heating at 85°C for 24 h.
Harvey Kaplan   +4 more
openaire   +5 more sources

XLMOD: Cross-linking and chromatography derivatization reagents ontology [PDF]

open access: yesarXiv, 2020
Mass spectrometry has experienced a rapid development since its first application for protein analysis in the 1980s. While the most common use of mass spectrometry for protein analysis is identification and quantification workflows on peptides (digested from their parent protein), there is also a rapidly growing use of mass spectrometry for structural ...
openaire   +3 more sources

A new radioactive cross-linking reagent for studying the interactions of proteins. [PDF]

open access: hybridJournal of Biological Chemistry, 1982
We have developed a photoactivable, heterobifunctional, reversible, radioactively labeled, chemical cross-linking reagent, 3-[(2-nitro-4-azidophenyl)-2-aminoethyldithio]-N-succinimidyl propionate, for studying the interactions of proteins in situ. When reacted in the dark with a purified protein, it forms a covalent derivative which can be purified and
Martin A. Schwartz   +2 more
openaire   +3 more sources

Effects of laccase and transglutaminase on the physicochemical and functional properties of hybrid lupin and whey protein powder [PDF]

open access: yesFoods
Plant-based protein is considered a sustainable protein source and has increased in demand recently. However, products containing plant-based proteins require further modification to achieve the desired functionalities akin to those present in animal ...
Chen, Tony   +11 more
core   +4 more sources

Designer Reagents for Mass Spectrometry-Based Proteomics: Clickable Cross-Linkers for Elucidation of Protein Structures and Interactions [PDF]

open access: green, 2012
We present novel homobifunctional amine-reactive clickable cross-linkers (CXLs) for investigation of three-dimensional protein structures and protein–protein interactions (PPIs).
Agnew, Heather D.   +11 more
core   +4 more sources

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