Determination of the degree of cross-linking of phenol-formaldehyde fibres

1983 ◽  
Vol 14 (6) ◽  
pp. 434-435
Author(s):  
S. G. Fedorkina ◽  
T. N. Koziorova ◽  
L. P. Chikalo
Keyword(s):  
Phenol Formaldehyde ◽  
Cross Linking

Determination of the degree of cross-linking of phenol-formaldehyde fibres

1982 ◽  
Vol 14 (6) ◽  
pp. 434-435
Author(s):  
S. G. Fedorkina ◽  
T. N. Koziorova ◽  
L. P. Chikalo
Keyword(s):  
Phenol Formaldehyde ◽  
Cross Linking

scholarly journals Determination of the Oligomeric State of SecYEG Protein Secretion Channel Complex Using in Vivo Photo- and Disulfide Cross-linking

2016 ◽  
Vol 291 (11) ◽  
pp. 5997-6010 ◽  
Author(s):  
Zeliang Zheng ◽  
Amy Blum ◽  
Tithi Banerjee ◽  
Qianyu Wang ◽  
Virginia Dantis ◽  
...  
Keyword(s):  
Protein Secretion ◽  
Cross Linking ◽  
Oligomeric State

scholarly journals Single-sided NMR for the measurement of the degree of cross-linking and curing

2018 ◽  
Vol 7 (1) ◽  
pp. 21-30 ◽  
Author(s):  
Norbert Halmen ◽  
Christoph Kugler ◽  
Eduard Kraus ◽  
Benjamin Baudrit ◽  
Thomas Hochrein ◽  
...  
Keyword(s):  
Relaxation Times ◽  
Curing Kinetics ◽  
Cross Linking ◽  
Scanning Calorimetry ◽  
First Results ◽  
Non Destructive ◽  
Kinetics Of ◽  
Good Agreement

Abstract. The degree of cross-linking and curing is one of the most important values concerning the quality of cross-linked polyethylene (PE-X) and the functionality of adhesives and resin-based components. Up to now, the measurement of this property has mostly been time-consuming and usually destructive. Within the shown work the feasibility of single-sided nuclear magnetic resonance (NMR) for the non-destructive determination of the degree of cross-linking and curing as process monitoring was investigated. First results indicate the possibility of distinguishing between PE-X samples with different degrees of cross-linking. The homogeneity of the samples and the curing kinetics of adhesives can also be monitored. The measurements show good agreement with reference tests (wet chemical analysis, differential scanning calorimetry, dielectric analysis). Furthermore, the influence of sample temperature on the characteristic relaxation times can be observed.

scholarly journals Analysis of protein-DNA interactions in chromatin by UV induced cross-linking and mass spectrometry

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Alexandra Stützer ◽  
Luisa M. Welp ◽  
Monika Raabe ◽  
Timo Sachsenberg ◽  
Christin Kappert ◽  
...  
Keyword(s):  
Uv Light ◽  
Amino Acid Level ◽  
Dna Interaction ◽  
Cross Linking ◽  
Dna Interactions ◽  
Single Experiment ◽  
Protein Dna Interactions ◽  
Nucleosome Binding ◽  
Binding Interfaces

Abstract Protein–DNA interactions are key to the functionality and stability of the genome. Identification and mapping of protein–DNA interaction interfaces and sites is crucial for understanding DNA-dependent processes. Here, we present a workflow that allows mass spectrometric (MS) identification of proteins in direct contact with DNA in reconstituted and native chromatin after cross-linking by ultraviolet (UV) light. Our approach enables the determination of contact interfaces at amino-acid level. With the example of chromatin-associated protein SCML2 we show that our technique allows differentiation of nucleosome-binding interfaces in distinct states. By UV cross-linking of isolated nuclei we determined the cross-linking sites of several factors including chromatin-modifying enzymes, demonstrating that our workflow is not restricted to reconstituted materials. As our approach can distinguish between protein–RNA and DNA interactions in one single experiment, we project that it will be possible to obtain insights into chromatin and its regulation in the future.

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