scholarly journals Synthesis of Tetrapeptide Derived from Skin Structural Protein Sequence and Identification of Skin Anti-aging Effect

2021 ◽  
Vol 27 (4) ◽  
pp. 231-238
Author(s):  
Sang Moon Kang ◽  
Yong-Seung Joun ◽  
Kee-Young Lee ◽  
Hyun Kang ◽  
Sung-Gyu Lee
Keyword(s):  
Protein Sequence ◽  
Aging Effect ◽  
Structural Protein

scholarly journals Adenovirus-associated Virus Structural Protein Sequence Homology

1979 ◽  
Vol 45 (1) ◽  
pp. 209-216 ◽  
Author(s):  
M. D. Lubeck ◽  
H. M. Lee ◽  
M. D. Hoggan ◽  
F. B. Johnson
Keyword(s):  
Sequence Homology ◽  
Protein Sequence ◽  
Structural Protein ◽  
Protein Sequence Homology

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

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