Cell-free Protein Synthesis in an Autoinduction System for NMR Studies of Protein–Protein Interactions

2005 ◽  
Vol 32 (3) ◽  
pp. 235-241 ◽  
Author(s):  
Kiyoshi Ozawa ◽  
Slobodan Jergic ◽  
Jeffrey A. Crowther ◽  
Phillip R. Thompson ◽  
Gene Wijffels ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Nmr Studies ◽  
Free Protein ◽  
Cell Free Protein Synthesis

scholarly journals Cell-free protein synthesis of perdeuterated proteins for NMR studies

2007 ◽  
Vol 39 (3) ◽  
pp. 229-238 ◽  
Author(s):  
Touraj Etezady-Esfarjani ◽  
Sebastian Hiller ◽  
Cristina Villalba ◽  
Kurt Wüthrich
Keyword(s):  
Protein Synthesis ◽  
Nmr Studies ◽  
Free Protein ◽  
Perdeuterated Proteins ◽  
Cell Free Protein Synthesis

NMR spectroscopy in the conformational analysis of peptides: an overview

2020 ◽  
Vol 27 ◽  
Author(s):  
Marian Vincenzi ◽  
Flavia Anna Mercurio ◽  
Marilisa Leone
Keyword(s):  
Nmr Spectroscopy ◽  
Protein Interactions ◽  
3D Structure ◽  
Theoretical Background ◽  
Triple Resonance ◽  
Protein Protein Interactions ◽  
Nmr Studies ◽  
Conformational Preferences ◽  
Dynamic Perspective ◽  
Nmr Methods

Background: NMR spectroscopy is one of the most powerful tools to study the structure and interaction properties of peptides and proteins from a dynamic perspective. Knowing the bioactive conformations of peptides is crucial in the drug discovery field to design more efficient analogue ligands and inhibitors of protein-protein interactions targeting therapeutically relevant systems. Objective: This review provides a toolkit to investigate peptide conformational properties by NMR. Methods: Articles cited herein, related to NMR studies of peptides and proteins were mainly searched through Pubmed and the web. More recent and old books on NMR spectroscopy written by eminent scientists in the field were consulted as well. Results: The review is mainly focused on NMR tools to gain the 3D structure of small unlabeled peptides. It is more application-oriented as it is beyond its goal to deliver a profound theoretical background. However, the basic principles of 2D homonuclear and heteronuclear experiments are briefly described. Protocols to obtain isotopically labeled peptides and principal triple resonance experiments needed to study them, are discussed as well. Conclusion: NMR is a leading technique in the study of conformational preferences of small flexible peptides whose structure can be often only described by an ensemble of conformations. Although NMR studies of peptides can be easily and fast performed by canonical protocols established a few decades ago, more recently we have assisted to tremendous improvements of NMR spectroscopy to investigate instead large systems and overcome its molecular weight limit.

scholarly journals Cell-free protein synthesis and in situ immobilization of deGFP-MatB in polymer microgels for malonate-to-malonyl CoA conversion

RSC Advances ◽  
2020 ◽  
Vol 10 (66) ◽  
pp. 40588-40596
Author(s):  
Tony Köhler ◽  
Thomas Heida ◽  
Sandra Hoefgen ◽  
Niclas Weigel ◽  
Vito Valiante ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Genetic Information ◽  
In Situ Immobilization ◽  
Bottom Up ◽  
Free Protein ◽  
Malonyl Coa ◽  
Cell Free Protein Synthesis

We describe a bottom-up approach towards functional enzymes utilizing microgels as carriers for genetic information that enable cell-free protein synthesis, in situ immobilization, and utilization of functional deGFP-MatB.

scholarly journals Multivariate statistical data analysis of cell‐free protein synthesis toward monitoring and control

AIChE Journal ◽  
2021 ◽  
Author(s):  
Carlos A. Duran‐Villalobos ◽  
Olotu Ogonah ◽  
Beatrice Melinek ◽  
Daniel G. Bracewell ◽  
Trevor Hallam ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Data Analysis ◽  
Statistical Data ◽  
Monitoring And Control ◽  
Statistical Data Analysis ◽  
Multivariate Statistical ◽  
Free Protein ◽  
And Control ◽  
Cell Free Protein Synthesis
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