scholarly journals Reprocessable polylactide-based networks containing urethane and disulfide linkages

2021 ◽  
pp. 110636
Author(s):  
Katarina Borska ◽  
Melania Bednarek ◽  
Andrzej Pawlak
Keyword(s):  
Disulfide Linkages

Cryo-electron microscopy of two-dimensional crystals of reduced type B botulinum neurotoxin

1992 ◽  
Vol 50 (1) ◽  
pp. 530-531
Author(s):  
P. F. Flicker ◽  
V.S. Kulkarni ◽  
J. P. Robinson ◽  
G. Stubbs ◽  
B. R. DasGupta
Keyword(s):  
Disulfide Bonds ◽  
Clostridium Botulinum ◽  
Structural Changes ◽  
Two Dimensional ◽  
Type B ◽  
Single Chain ◽  
Muscle Paralysis ◽  
Cryo Electron Microscopy ◽  
Disulfide Linkages ◽  
Intracellular Action

Botulinum toxin is a potent neurotoxin produced by Clostridium botulinum. The toxin inhibits release of neurotransmitter, causing muscle paralysis. There are several serotypes, A to G, all of molecular weight about 150,000. The protein exists as a single chain or or as two chains, with two disulfide linkages. In a recent investigation on intracellular action of neurotoxins it was reported that type B neurotoxin can inhibit the release of Ca++-activated [3H] norepinephrine only if the disulfide bonds are reduced. In order to investigate possible structural changes in the toxin upon reduction of the disulfide bonds, we have prepared two-dimensional crystals of reduced type B neurotoxin. These two-dimensional crystals will be compared with those of the native (unreduced) type B toxin.

Role of disulfide linkages in tachyplesin-lipid interactions

Biochemistry ◽  
1993 ◽  
Vol 32 (43) ◽  
pp. 11704-11710 ◽  
Author(s):  
Katsumi Matsuzaki ◽  
Mitsuya Nakayama ◽  
Masaru Fukui ◽  
Akira Otaka ◽  
Susumu Funakoshi ◽  
...  
Keyword(s):  
Lipid Interactions ◽  
Disulfide Linkages

A reversible supramolecular assembly containing ionic interactions and disulfide linkages

2014 ◽  
Vol 38 (11) ◽  
pp. 5186-5189 ◽  
Author(s):  
Xinrong Lin ◽  
Guilhem Godeau ◽  
Mark W. Grinstaff
Keyword(s):  
Redox Reaction ◽  
Supramolecular Assembly ◽  
Ionic Interactions ◽  
Cooling Cycle ◽  
Disulfide Linkages

A reversible ionic supramolecular assembly is described which can be disrupted and reformed by application of either a heating–cooling cycle or a mild redox reaction.

A small v-sis/platelet-derived growth factor (PDGF) B-protein domain in which subtle conformational changes abrogate PDGF receptor interaction and transforming activity

1990 ◽  
Vol 10 (10) ◽  
pp. 5496-5501
Author(s):  
N Giese ◽  
W J LaRochelle ◽  
M May-Siroff ◽  
K C Robbins ◽  
S A Aaronson
Keyword(s):  
Monoclonal Antibody ◽  
Growth Factor ◽  
Conformational Changes ◽  
Protein Domain ◽  
Platelet Derived Growth Factor ◽  
Receptor Interaction ◽  
Pdgf Receptor ◽  
Amino Acid Residues ◽  
Disulfide Linkages ◽  
Transforming Activity

Deletion scanning mutagenesis within the transforming region of the v-sis oncogene was used to dissect structure-function relationships. Mutations affecting codons within a domain encoding amino acids 136 through 148 had no effect upon homodimer formation or recognition by antisera which detect determinants dependent upon native intrachain disulfide linkages, yet the same mutations completely abolished transforming activity. A platelet-derived growth factor B (PDGF B) monoclonal antibody that prevents its interaction with PDGF receptors recognized v-sis, delta 142 (deletion of codon 142), and delta 148 but not delta 136, delta 137, or delta 139 mutants. These findings mapped the epitope recognized by this monoclonal antibody to include amino acid residues 136 to 139. Furthermore, mutations in the codon 136 to 148 domain caused markedly impaired ability to induce PDGF receptor tyrosine phosphorylation. Thus, subtle conformational alterations in this small domain critically affect PDGF receptor recognition and/or functional activation.

Low Temperature Expansion of Polysulfide Rubbers

1966 ◽  
Vol 39 (2) ◽  
pp. 211-216
Author(s):  
B. A. Hunter ◽  
M. J. Kleinfeld
Keyword(s):  
Room Temperature ◽  
Liquid Mixture ◽  
Cumene Hydroperoxide ◽  
Polymer Chains ◽  
Nitrogen Gas ◽  
Blowing Agents ◽  
Disulfide Linkages ◽  
Novel Method ◽  
Rubber Product ◽  
Liquid Polysulfide Rubbers

Abstract A novel method for producing a cellular cured rubber product at room temperature has been developed. Pourable liquid polysulfide polymers are treated with a conventional oxidizing curative and selected water-sensitive or oxidation-sensitive blowing agents. Standing at ambient temperature the viscous liquid mixture gradually “rises” and cures to form a finely porous cellular rubber product. Conventional curatives employed include oxidizing agents such as lead peroxide and cumene hydroperoxide. These convert terminal or pendant thiol groups in the polysulfide polymer chains to chain-connecting disulfide linkages. Water is a byproduct of the curing reaction. In the presence of water-sensitive blowing agents such as, (1) metal salts of azodicarboxylic acid or, (2) metal hydride compounds the water produced in the cure reacts to form copious amounts of nitrogen or of hydrogen. Alternatively, oxidation-sensitive blowing agents such as p, p′-oxybis-(benzene sulfonyl hydrazide) react directly with the oxidizing curative to form nitrogen gas. The blowing reactions are concurrent with cure and efficient and controllable expansion can be achieved. The unique process offers possible economies and special properties in applications of liquid polysulfide rubbers as potting compounds, joint sealants, solvent resistant forms, and cold casting compounds.

scholarly journals Sindbis Virus Glycoprotein E1 Is Divided into Two Discrete Domains at Amino Acid 129 by Disulfide Bridge Connections

2000 ◽  
Vol 74 (19) ◽  
pp. 9313-9316 ◽  
Author(s):  
Brett S. Phinney ◽  
Dennis T. Brown
Keyword(s):  
Amino Acid ◽  
Disulfide Bonds ◽  
Sindbis Virus ◽  
Disulfide Bridge ◽  
Membrane Glycoprotein ◽  
Disulfide Bridges ◽  
Functional Regions ◽  
E1 Protein ◽  
Disulfide Linkages ◽  
Discrete Domains

ABSTRACT The E1 membrane glycoprotein of Sindbis virus contains structural and functional domains, which are conformationally dependent on the presence of intramolecular disulfide bridges (B. A. Abell and D. T. Brown, J. Virol. 67:5496–5501, 1993; R. P. Anthony, A. M. Paredes, and D. T. Brown, Virology 190:330–336, 1992). We have examined the disulfide bonds in E1 and have determined that the E1 membrane glycoprotein contains two separate sets of interconnecting disulfide linkages, which divide the protein into two domains at amino acid 129. These separate sets of disulfides may stabilize and define the structural and functional regions of the E1 protein.

scholarly journals Characterization of Disulfide Linkages in Proteins by 193 nm Ultraviolet Photodissociation (UVPD) Mass Spectrometry

2018 ◽  
Vol 90 (14) ◽  
pp. 8523-8530 ◽  
Author(s):  
M. Montana Quick ◽  
Christopher M. Crittenden ◽  
Jake A. Rosenberg ◽  
Jennifer S. Brodbelt
Keyword(s):  
Mass Spectrometry ◽  
Ultraviolet Photodissociation ◽  
Disulfide Linkages ◽  
193 Nm
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