Investigation of the new substitution glycine to alaninewithin the Kringle-2 domain of reteplase: a molecular dynamics study

The conformational stability of r-PA conferred by glycine replacement with alanine may decrease the propensity for proteolysis in protease - rich environments across various recombinant systems and potentially enhance its production and expression levels.

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Publication Details

Journal
BioTechnologia
Published
2024-09-30
DOI
https://doi.org/10.5114/bta.2024.141801
Citations
2
Primary Topic
Enzyme Structure and Function
Type
article
Field-Weighted Citation Impact
0.23

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article

Investigation of the new substitution glycine to alaninewithin the Kringle-2 domain of reteplase: a molecular dynamics study

Mokhtar Jalali Javaran, Kaveh Haji-Allahverdipoor, Mohamad Bagher Khadem-Erfan, Habib Eslami et al.
2 citations
BioTechnologia
Enzyme Structure and Function
0.23
article

Investigation of the new substitution glycine to alaninewithin the Kringle-2 domain of reteplase: a molecular dynamics study

Mokhtar Jalali Javaran, Kaveh Haji-Allahverdipoor, Mohamad Bagher Khadem-Erfan, Habib Eslami, Sajad Rashidi Monfared, Koosha Rokhzadi
article en
2 citations

Abstract

The conformational stability of r-PA conferred by glycine replacement with alanine may decrease the propensity for proteolysis in protease - rich environments across various recombinant systems and potentially enhance its production and expression levels.

BioTechnologiaVol. 105(3)
Tarbiat Modares University (IR), Kurdistan University of Medical Sciences (IR), Hormozgan University of Medical Sciences (IR)
Tarbiat Modares University, Kurdistan University Of Medical Sciences
Openalex Percentile: Top 51%
Enzyme Structure and Function
0.23
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