Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters











Database
Language
Publication year range
1.
J Oleo Sci ; 62(3): 123-32, 2013.
Article in English | MEDLINE | ID: mdl-23470439

ABSTRACT

Hydrogen bonding between surfactant molecules plays an important role in self-assembly formation. For long alkyl chain amine oxide surfactants, the specific protonation degree dependence of some solution properties has been considered to be due to hydrogen bonding between protonated and deprotonated species. In addition to this type of hydrogen bonding, we introduced a pyridyl group into an alkylamine oxide molecule as a new hydrogen-bonding site. The pyridyl group has three different structural isomers based on the position of the substituent. An amine oxide group in pyridylamine oxides was preferentially protonated. In addition, protonation of the pyridyl group revealed a pronounced substituent position effect on the critical micelle concentration, micellar size, and solubilization of oil-soluble dye into micelles. The intermolecular or intramolecular hydrogen bond formation could be controlled by altering the substituent position.


Subject(s)
Amines/chemistry , Oxides/chemistry , Pyridines/chemistry , Surface-Active Agents/chemistry , Hydrogen Bonding , Molecular Structure , Protons , Solutions
2.
EMBO J ; 15(3): 457-67, 1996 Feb 01.
Article in English | MEDLINE | ID: mdl-8599929

ABSTRACT

Microtubule-associated motor proteins are thought to be involved in spindle formation and chromosome movements in mitosis/meiosis. We have molecularly cloned cDNAs for a gene that codes for a novel member of the kinesin family of proteins. Nucleotide sequencing reveals that the predicted gene product is a 73 kDa protein and is related to some extent to the Drosophila node gene product, which is involved in chromosomal segregation during meiosis. A sequence similar to the microtubule binding motor domain of kinesin is present in the N-terminal half of the protein, and its ability to bind to microtubules is demonstrated. Furthermore we show that its C-terminal half contains a putative nuclear localization signal similar to that of Jun and is able to bind to DNA. Accordingly, the protein was termed Kid (kinesin-like DNA binding protein). Indirect immunofluorescence studies show that Kid colocalizes with mitotic chromosomes and that it is enriched in the kinetochore at anaphase. Thus, we propose that Kid might play a role(s) in regulating the chromosomal movement along microtubules during mitosis.


Subject(s)
DNA-Binding Proteins/genetics , DNA-Binding Proteins/metabolism , Drosophila Proteins , Kinesins/genetics , Kinesins/metabolism , Microtubule-Associated Proteins/genetics , Microtubule-Associated Proteins/metabolism , Amino Acid Sequence , Animals , Base Sequence , Breast Neoplasms/genetics , Chromosomes, Human/metabolism , Cloning, Molecular , DNA, Complementary/genetics , DNA-Binding Proteins/chemistry , Drosophila/genetics , Female , HeLa Cells , Humans , Kinesins/chemistry , Microtubule Proteins/genetics , Microtubule-Associated Proteins/chemistry , Mitosis , Molecular Sequence Data , Molecular Weight , Sequence Homology, Amino Acid , Spindle Apparatus/metabolism , Tumor Cells, Cultured
SELECTION OF CITATIONS
SEARCH DETAIL