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Biomedical subjects

Q X Jiang

Publications and source records attributed to Q X Jiang.

5 recordsLinked to original sources

[Study of improving professional training: effect on data collection].

In this study, 30 nurses who worked and studied in one ward were divided into three groups. They accepted one of the three measures for training, that is, lecture, teach by demonstration, and pre-practice and after practice discussion. The quality of data collecting process and data records for everyone have been checked. Result showed the quality of three groups got progress by training and the group of discussion was the best. The progress was increasing obviously with time of work and education.

Education, Nursing, Continuing↗

[Analysis of relative factors on paralytic patients with pressure sore complications].

In this study, risk factors for bedsore were studied on 100 paralytic patients with neurologic diseases. The patient's assessment scores based on the risk factors for bedsore were evaluated and analyzed. According to the result, the critical point of assessment score for bedsore was established. The patient will be put into the high risk group of bedsore if his/her assessment score is higher than the critical point and special nursing intervention will be given.

Female↗

Interactions of both melittin and its site-specific mutants with bacteriorhodopsin of Halobacterium halobium: sites of electrostatic interaction on melittin.

Melittin and its site-specific mutants differentially delay the slow-decaying component of the photocycle intermediate M412 of bacteriorhodopsin in the purple membrane and the acetylated purple membrane whose several lysine residues are modified. This effect is attributed to the interaction of the total positive charges of melittin or its mutants with the total negative charges of bacteriorhodopsin. The effects of melittin and its mutants on the Triton X-100-solubilized bacteriorhodopsin monomers are somewhat complicated but are associated with their charges. These results show that there is electrostatic interaction between bacteriorhodopsin and melittin and that both N- and C-termini of melittin function as sites of the interaction, with Arg 22 and Arg 24 making a prominent contribution to the effective surface charge of melittin. Melittin, at certain concentrations, partially restores the decreased photoactivity of the bacteriorhodopsin monomers trapped in the Triton-lipid-protein mixed micelles, which suggests that melittin may compete with Triton X-100 for the binding sites on the bacteriorhodopsin monomers. Other kinds of interactions between bacteriorhodopsin and melittin are also indicated. The possible states of melittin in membranes are discussed.

Amino Acid Sequence↗

Spherical reconstruction: a method for structure determination of membrane proteins from cryo-EM images.

We propose a new method for single-particle reconstruction, which should be generally applicable to structure determination for membrane proteins. After reconstitution into a small spherical vesicle, a membrane protein takes a particular orientation relative to the membrane normal, and its position in the projected image of the vesicle directly defines two of its three Euler angles of orientation. The spherical constraint imposed by the vesicle effectively reduces the dimensionality of the alignment search from 5 to 3 and simplifies the detection of the particle. Projection images of particles in vesicles collectively take all possible orientations and therefore cover the whole Fourier space. Analysis of images of vesicles in ice showed that the vesicle density is well described by a simple model for membrane electron scattering density. In fitting this model we found that osmotically swollen vesicles remain nearly spherical through the freezing process. These results satisfy the basic experimental requirements for spherical reconstruction. A computer simulation of particles in vesicles showed that this method provides good estimates of the two Euler angles and thus may improve single-particle reconstruction and extend it to smaller membrane proteins.

Animals↗