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Moreover, we propose a conceptual framework that allows us to quantify the relationship between sequence, structure, and binding energetics.
Many functions have been developed to quantify the structural and energetic properties of interacting proteins, finding use in interrelated challenges revolving around the relationship between sequence, structure and binding free energy.
Taken together, these observations show that the relationship between sequence, structure, and function is complex.
This absence of a simple relationship between sequence, structure and binding specificity, coupled to the low level of sequence conservation between KAP-βs, makes determining the evolutionary origins and history of KAP-βs challenging.
It is expected that understanding the relationships between sequence, structure and function would greatly help the engineering of laccases.
In the case of mechanical proteins, the understanding of the relationship between sequence, structure, and mechanical properties is incomplete.
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Identification of the critical determinants of the two different EF-hand domain arrangements and the distinct dynamical features relevant to their respective functions provides insight into the relationships between sequence, structure, dynamics and function among these EF-hand CaBPs.
Comparative genomics holds tremendous promises to fill the gap between sequence, structure, function and evolution.
Recent studies are beginning to explore the relationship between peptoid sequence, structure and function.
These models are powerful because they capture higher order correlations induced by mutations evolving under constraints and help quantify the connections between protein sequence, structure, and function maintained through evolution.
MS-based proteomics has also been widely applied to structural biology, where proteomic investigation is being used to improve knowledge on the relationship between protein sequence, structure, and function.
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