Janos H. Fendler, Membrane Mimetic Chemistry, Clarkson College of Technology, Wiley, London (1982) 522 p..

This research is an examination and a study on the influence of rewards on job satisfaction of lecturers at Shinas College of Technology (ShCT). In academic industry, rewards are one of the factors that affecting job satisfaction of the employees and this will lead to affect their performance in their jobs. So, when rewards are more the job satisfaction will be high and when rewards are less the job satisfaction will be less. On the other hand, the age will not affect the job satisfaction. Previous research reveals that Job satisfaction is very important to success the industry and the rewards are the main factors which affect job satisfaction. The main purpose of this study is to know the influence of rewards in job satisfaction among the lecturers in ShCT. Moreover, this research attempts to identify how much rewards affect the job satisfaction in ShCT. For this study used two types of data which are: primary data and secondary data. The sources of primary data is the response from lecturers at ShCT. It is collected through structured questionnaire and distributed such to 60 respondents. Secondary data, collected from internet, books, journals, articles etc.

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Surface-Bound Membrane-Mimetic Assemblies: Electrostatic Attributes of Integral Membrane Proteins

10.21236/ada204381 ◽

1988 ◽

Author(s):

H. G. Smith

Keyword(s):

Membrane Proteins ◽

Integral Membrane Proteins ◽

Membrane Mimetic

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Synthesis and Characterization of Folate-Modified Cell Membrane Mimetic Copolymer Micelles for Effective Tumor Cell Internalization

ACS Applied Bio Materials ◽

10.1021/acsabm.0c01612 ◽

2021 ◽

Author(s):

Wei Du ◽

Qian Lu ◽

Mengchen Zhang ◽

Haimei Cao ◽

Shiping Zhang

Keyword(s):

Cell Membrane ◽

Tumor Cell ◽

Synthesis And Characterization ◽

Cell Internalization ◽

Membrane Mimetic ◽

Copolymer Micelles

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CryoEM structure of the antibacterial target PBP1b at 3.3 Å resolution

Nature Communications ◽

10.1038/s41467-021-23063-6 ◽

2021 ◽

Vol 12 (1) ◽

Author(s):

Nathanael A. Caveney ◽

Sean D. Workman ◽

Rui Yan ◽

Claire E. Atkinson ◽

Zhiheng Yu ◽

...

Keyword(s):

Electron Microscopy ◽

Acid Anhydride ◽

Atomic Resolution ◽

Inherent Difficulty ◽

Penicillin Binding Proteins ◽

Antibiotic Development ◽

Class A ◽

Membrane Mimetic ◽

Antibacterial Target ◽

Resolution Structure

AbstractThe pathway for the biosynthesis of the bacterial cell wall is one of the most prolific antibiotic targets, exemplified by the widespread use of β-lactam antibiotics. Despite this, our structural understanding of class A penicillin binding proteins, which perform the last two steps in this pathway, is incomplete due to the inherent difficulty in their crystallization and the complexity of their substrates. Here, we determine the near atomic resolution structure of the 83 kDa class A PBP from Escherichia coli, PBP1b, using cryogenic electron microscopy and a styrene maleic acid anhydride membrane mimetic. PBP1b, in its apo form, is seen to exhibit a distinct conformation in comparison to Moenomycin-bound crystal structures. The work herein paves the way for the use of cryoEM in structure-guided antibiotic development for this notoriously difficult to crystalize class of proteins and their complex substrates.

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