scholarly journals Calorimetric study of a series of designed repeat proteins: Modular structure and modular folding

2011 ◽  
Vol 20 (2) ◽  
pp. 336-340 ◽  
Author(s):  
Aitziber L. Cortajarena ◽  
Lynne Regan
Keyword(s):  
Modular Structure ◽  
Calorimetric Study ◽  
Repeat Proteins

Repeat proteins challenge the concept of structural domains

2015 ◽  
Vol 43 (5) ◽  
pp. 844-849 ◽  
Author(s):  
Rocío Espada ◽  
R. Gonzalo Parra ◽  
Manfred J. Sippl ◽  
Thierry Mora ◽  
Aleksandra M. Walczak ◽  
...  
Keyword(s):  
Biological Systems ◽  
Modular Structure ◽  
Structural Domains ◽  
Repeat Array ◽  
Repeat Units ◽  
Repeat Proteins ◽  
Folding Dynamics ◽  
And Function

Structural domains are believed to be modules within proteins that can fold and function independently. Some proteins show tandem repetitions of apparent modular structure that do not fold independently, but rather co-operate in stabilizing structural forms that comprise several repeat-units. For many natural repeat-proteins, it has been shown that weak energetic links between repeats lead to the breakdown of co-operativity and the appearance of folding sub-domains within an apparently regular repeat array. The quasi-1D architecture of repeat-proteins is crucial in detailing how the local energetic balances can modulate the folding dynamics of these proteins, which can be related to the physiological behaviour of these ubiquitous biological systems.

In silico Defining the Repeat-containing Proteins in the Acinetobacter baumannii Proteome, a Great Reservoir of Templates for Synthetic Biology

2019 ◽  
Vol 13 (2) ◽  
pp. 149-158
Author(s):  
Mohammad Reza Rahbar ◽  
Mahboubeh Zarei ◽  
Navid Nezafat ◽  
Manica Negahdaripour ◽  
Younes Ghasemi
Keyword(s):  
Acinetobacter Baumannii ◽  
Drug Targets ◽  
Closely Related Species ◽  
Great Ability ◽  
Repeat Proteins ◽  
Significant Difference ◽  
Biological Determinants ◽  
Tandem Repeat Proteins ◽  
Diagnostic Approaches ◽  
Novel Therapeutic

Background: Acinetobacter baumannii is an important nosocomial pathogen with great ability to resist antibiotics. Tandem repeat proteins, abundant in prokaryotic proteomes, attract attention due to their role in virulence and various biological processes. Defining repeat- containing proteins may pave the way to find novel therapeutic targets as well as vaccine candidate and give pieces of evidence of mechanisms of evolution and adaptation of organisms to various environmental conditions. Objective: In the present study, we employed bioinformatics tools to define repeatcontaining proteins within A. baumannii proteome for emphasizing the existence of natural sources for synthesizing novel therapeutic and diagnosis material. Results: We defined various kinds of repeat modules in a number of proteins and compared the abundance of these proteins in some closely related species. No significant difference was observed in the count of repeat-containing proteins in different species. But the existence of some important virulence factors is mentionable in our screening. Conclusion: Repeat containing proteins are important biological determinants of A. baumannii and are well worth researching for finding drug targets and vaccine candidates. These proteins can be served as a template for designing and synthesizing peptides for therapeutic and diagnostic approaches.

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