Fluorophore Appended Saccharide Cyclophane:  Self-Association, Fluorescent Properties, Heterodimers with Cyclodextrins, and Cross-Linking Behavior with Peanut Agglutinin of Dansyl-Modified Saccharide Cyclophane

2004 ◽  
Vol 69 (10) ◽  
pp. 3509-3516 ◽  
Author(s):  
Osamu Hayashida ◽  
Itaru Hamachi
Keyword(s):  
Cross Linking ◽  
Peanut Agglutinin ◽  
Fluorescent Properties ◽  
Self Association

scholarly journals A gamma Gly-268 to Glu substitution is responsible for impaired fibrin assembly in a homozygous dysfibrinogen Kurashiki I

Blood ◽  
1996 ◽  
Vol 87 (11) ◽  
pp. 4686-4694 ◽  
Author(s):  
K Niwa ◽  
M Takebe ◽  
T Sugo ◽  
Y Kawata ◽  
J Mimuro ◽  
...  
Keyword(s):  
Tissue Type ◽  
Factor Xiiia ◽  
Cross Linking ◽  
Fibrin Gel ◽  
Functional Abnormality ◽  
Human Fibrinogen ◽  
Fibrin Monomer ◽  
Longitudinal Association ◽  
Self Association ◽  
A Site

A new type of gamma Gly-268 (GGA) to Glu (GAA) substitution has been identified in a homozygous dysfibrinogen by analyses of the affected polypeptide and its encoding gene derived from a 58 year-old man manifesting no major bleeding or thrombosis. The functional abnormality was characterized by impaired fibrin assembly most likely due to failure to construct properly aligned double-stranded fibrin protofibrils. This presumption was deduced from the following findings: (1) Factor XIIIa-catalyzed cross-linking of the fibrin gamma-chains progressed in a normal fashion, indicating that the contact between the central E domain of one fibrin monomer and the D domain of another took place normally; (2) Nevertheless, factor XIIIa-catalyzed cross-linking of the fibrinogen gamma-chains was obviously delayed, suggesting that longitudinal association of D domains of different fibrin monomers, ie, D:D association was perturbed; (3) Plasminogen activation catalyzed by tissue-type plasminogen activator was not as efficiently facilitated by polymerizing fibrin monomer derived from the patient as by the normal counterpart. Therefore, gamma Gly-268 would not be involved in the 'a' site residing in the D domain, which functions as a complementary binding site with the thrombin-activated 'A' site in the central E domain, but would be rather involved in the D:D self association sites recently proposed for human fibrinogen. Thus, the gamma Glu-268 substitution newly identified in this homozygous dysfibrinogen seems to impair proper alignment of adjacent D domains of neighboring fibrin molecules in the double-stranded fibrin protofibril, resulting in delayed fibrin gel formation.

Distinct Steps of Cross-linking, Self-association, and Maturation of Tropoelastin Are Necessary for Elastic Fiber Formation

2007 ◽  
Vol 369 (3) ◽  
pp. 841-851 ◽  
Author(s):  
Fumiaki Sato ◽  
Hiroshi Wachi ◽  
Marie Ishida ◽  
Risa Nonaka ◽  
Satoshi Onoue ◽  
...  
Keyword(s):  
Elastic Fiber ◽  
Fiber Formation ◽  
Cross Linking ◽  
Self Association

scholarly journals Covalent cross-linking of the bovine somatotropin dimer. Effects on growth-promoting, receptor-binding and immunological activities and preliminary characterization of the self-association

1983 ◽  
Vol 209 (1) ◽  
pp. 107-115 ◽  
Author(s):  
H N Fernández ◽  
J M Delfino
Keyword(s):  
Critical Role ◽  
The Self ◽  
Bovine Somatotropin ◽  
Cross Linking ◽  
British Library ◽  
Dimethyl Suberimidate ◽  
Growth Promoting ◽  
Self Association

Bovine somatotropin, at pH 8.5 in 0.02 M-Bicine [NN-bis-(2-hydroxyethyl)glycine]/0.09M-NaCl, showed by frontal analysis the characteristics of a rapid monomer-dimer equilibrium whose dissociation constant was estimated to be 6.6×10(-6)M. Reaction of the hormone with dimethyl suberimidate lead to covalent cross-linking of the dimeric species. Under the conditions chosen (0.4 mg of bifunctional imidate and 1 mg of protein/ml at room temperature for 1 h) the cross-linked dimers accounted for 26% of the total protein, and these were isolated by molecular sieving in 0.29M-NH3/0.12M-NaCl. Covalent stabilization greatly diminished the growth-promoting activity and the ability to interact with somatogenic sites in both rat liver in vivo and rabbit liver microsomal fractions. Evidence indicating a non-critical role for amino groups involved in the covalent cross-linking was provided by a nearly equivalent derivative obtained after reaction with 3,3′-dithiobispropionimidate, which had substantial hormonal activity upon cleavage of the disulphide links. Conversely, immunological reactivity as demonstrated by radioimmunoassay was not affected by cross-linking. Details of the least-squares procedure employed to evaluate the self-association equilibrium constant has been deposited as Supplement SUP 50115 (7 pages) with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms indicated in Biochem. J. (1981) 193,5.

scholarly journals P1 ParB Domain Structure Includes Two Independent Multimerization Domains

1999 ◽  
Vol 181 (19) ◽  
pp. 5898-5908 ◽  
Author(s):  
Jennifer A. Surtees ◽  
Barbara E. Funnell
Keyword(s):  
Amino Acids ◽  
Domain Structure ◽  
Cross Linking ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
C Terminus ◽  
Self Association ◽  
Two Hybrid ◽  
Chemical Cross Linking

ABSTRACT ParB is one of two P1-encoded proteins that are required for active partition of the P1 prophage in Escherichia coli. To probe the native domain structure of ParB, we performed limited proteolytic digestions of full-length ParB, as well as of several N-terminal and C-terminal deletion fragments of ParB. The C-terminal 140 amino acids of ParB form a very trypsin-resistant domain. In contrast, the N terminus is more susceptible to proteolysis, suggesting that it forms a less stably folded domain or domains. Because native ParB is a dimer in solution, we analyzed the ability of ParB fragments to dimerize, using both the yeast two-hybrid system and in vitro chemical cross-linking of purified proteins. These studies revealed that the C-terminal 59 amino acids of ParB, a region within the protease-resistant domain, are sufficient for dimerization. Cross-linking and yeast two-hybrid experiments also revealed the presence of a second self-association domain within the N-terminal half of ParB. The cross-linking data also suggest that the C terminus is inhibitory to multimerization through the N-terminal domain in vitro. We propose that the two multimerization domains play distinct roles in partition complex formation.

Self-association of casein studied using enzymatic cross-linking at different temperatures

2019 ◽  
Vol 28 ◽  
pp. 89-98 ◽  
Author(s):  
Norbert Raak ◽  
Lena Brehm ◽  
Raffaele Andrea Abbate ◽  
Thomas Henle ◽  
Albena Lederer ◽  
...  
Keyword(s):  
Cross Linking ◽  
Different Temperatures ◽  
Self Association

scholarly journals The H3 Tail Domain Participates in Multiple Interactions during Folding and Self-Association of Nucleosome Arrays

2007 ◽  
Vol 27 (6) ◽  
pp. 2084-2091 ◽  
Author(s):  
Pu-Yeh Kan ◽  
Xu Lu ◽  
Jeffrey C. Hansen ◽  
Jeffrey J. Hayes
Keyword(s):  
Short Range ◽  
Chromatin Condensation ◽  
Cross Linking ◽  
Tail Domain ◽  
Histone Tail ◽  
Linker Histones ◽  
Complex Interactions ◽  
Self Association ◽  
Core Histone Tail ◽  
Nucleosome Arrays

ABSTRACT The core histone tail domains play a central role in chromatin structure and epigenetic processes controlling gene expression. Although little is known regarding the molecular details of tail interactions, it is likely that they participate in both short-range and long-range interactions between nucleosomes. Previously, we demonstrated that the H3 tail domain participates in internucleosome interactions during MgCl2-dependent condensation of model nucleosome arrays. However, these studies did not distinguish whether these internucleosome interactions represented short-range intra-array or longer-range interarray interactions. To better understand the complex interactions of the H3 tail domain during chromatin condensation, we have developed a new site-directed cross-linking method to identify and quantify interarray interactions mediated by histone tail domains. Interarray cross-linking was undetectable under salt conditions that induced only local folding, but was detected concomitant with salt-dependent interarray oligomerization at higher MgCl2 concentrations. Interestingly, lysine-to-glutamine mutations in the H3 tail domain to mimic acetylation resulted in little or no reduction in interarray cross-linking. In contrast, binding of a linker histone caused a much greater enhancement of interarray interactions for unmodified H3 tails compared to “acetylated” H3 tails. Collectively these results indicate that H3 tail domain performs multiple functions during chromatin condensation via distinct molecular interactions that can be differentially regulated by acetylation or binding of linker histones.

scholarly journals Domain swap in the C-terminal ubiquitin-like domain of human doublecortin

2018 ◽  
Vol 74 (5) ◽  
pp. 450-462 ◽  
Author(s):  
Arne C. Rufer ◽  
Eric Kusznir ◽  
Dominique Burger ◽  
Martine Stihle ◽  
Armin Ruf ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Analytical Ultracentrifugation ◽  
Cross Linking ◽  
Cooperative Binding ◽  
Domain Swap ◽  
Microtubule Polymerization ◽  
Open Conformation ◽  
Double Cortex Syndrome ◽  
Double Cortex ◽  
Self Association

Doublecortin, a microtubule-associated protein that is only produced during neurogenesis, cooperatively binds to microtubules and stimulates microtubule polymerization and cross-linking by unknown mechanisms. A domain swap is observed in the crystal structure of the C-terminal domain of doublecortin. As determined by analytical ultracentrifugation, an open conformation is also present in solution. At higher concentrations, higher-order oligomers of the domain are formed. The domain swap and additional interfaces observed in the crystal lattice can explain the formation of doublecortin tetramers or multimers, in line with the analytical ultracentrifugation data. Taken together, the domain swap offers a mechanism for the observed cooperative binding of doublecortin to microtubules. Doublecortin-induced cross-linking of microtubules can be explained by the same mechanism. The effect of several mutations leading to lissencephaly and double-cortex syndrome can be traced to the domain swap and the proposed self-association of doublecortin.

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