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4. Functional inhibition: The function of many proteins is the inhibition or delay of processes that lead to cell growth.
Prenylation is a posttranslational modification essential for the proper localization and function of many proteins.
The folding, structure and biological function of many proteins are inherently dynamic properties of the protein molecule.
Although internal water molecules are essential for the structure and function of many proteins, the structural and physical factors that govern internal hydration are poorly understood.
Since surface tension is known to modulate the function of many proteins, this effect is an important consideration for predictions of ion channel function.
Small molecule recognition is critical to the function of many proteins; therefore, determination of ligand binding site similarity is important for understanding ligand interactions and may allow their functional classification.
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In addition, the function of many protein kinases is completely unknown or has been poorly characterized.
As shown, the function of many protein-coding genes associated with species-specific repeats remains unknown.
Since these approaches have generally been used to assess dynamic events of relatively small amplitude, it was necessary to derive a means of extending these methods to enable the description of the large conformational interconversions associated with the function of many protein molecules.
The availability of the genome sequence of Mycobacterium tuberculosis H37Rv has encouraged determination of large numbers of protein structures and detailed definition of the biological information encoded therein; yet, the functions of many proteins in M. tuberculosis remain unknown.
The functions of many proteins that appear to be redundant under typical conditions may be revealed under conditions where the system is sensitised or stressed.
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