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The isoelectric point or pI of a protein corresponds to the solution pH at which the net surface charge is zero. In the denatured state, the pI depends solely on a protein’s amino acid composition. Since the earliest days of solution biochemistry, the pI has been recorded and reported. Literature reports of pI abound. The protein isoelectric point database (PIP-DB) has collected and collated this legacy data to provide an increasingly comprehensive database for comparison and benchmarking purposes.

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The isoelectric point or pI of a protein corresponds to the solution pH at which the net surface charge is zero. In the denatured state, the pI depends solely on a protein’s amino acid composition. Since the earliest days of solution biochemistry, the pI has been recorded and reported. Literature reports of pI abound. The protein isoelectric point database (PIP-DB) has collected and collated this legacy data to provide an increasingly comprehensive database for comparison and benchmarking purposes.
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pip-db | pip-db.org Reviews

https://pip-db.org

The isoelectric point or pI of a protein corresponds to the solution pH at which the net surface charge is zero. In the denatured state, the pI depends solely on a protein’s amino acid composition. Since the earliest days of solution biochemistry, the pI has been recorded and reported. Literature reports of pI abound. The protein isoelectric point database (PIP-DB) has collected and collated this legacy data to provide an increasingly comprehensive database for comparison and benchmarking purposes.

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The isoelectric point or pI of a protein corresponds to the solution pH at which the net surface charge is zero. In the denatured state, the pI depends solely on a protein’s amino acid composition. Since the earliest days of solution biochemistry, the pI has been recorded and reported. Literature reports of pI abound. The protein isoelectric point database (PIP-DB) has collected and collated this legacy data to provide an increasingly comprehensive database for comparison and benchmarking purposes.

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