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Very fast empirical prediction and rationalization of protein pKa values

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Very fast empirical prediction and rationalization of protein pKa values (English)

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Li H

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1

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Jensen JH

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1 December 2005

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61

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4

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704-21

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cites work

Electrostatic models for computing protonation and redox equilibria in proteins.

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Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.20660

retrieved

21 January 2018

pK a Prediction for Organic Acids and Bases

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Crossref

reference URL

https://api.crossref.org/works/10.1002%2FPROT.20660

retrieved

21 January 2018

Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design

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Crossref

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https://api.crossref.org/works/10.1002%2FPROT.20660

retrieved

21 January 2018

Ionization properties of titratable groups in ribonuclease T1. I. pKa values in the native state determined by two-dimensional heteronuclear NMR spectroscopy

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https://api.crossref.org/works/10.1002%2FPROT.20660

retrieved

21 January 2018

Thermodynamic linkage between the binding of protons and inhibitors to HIV-1 protease

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https://api.crossref.org/works/10.1002%2FPROT.20660

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21 January 2018

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

557952

OpenCitations bibliographic resource ID

557952

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Consolidated OpenCitations Corpus – April 2017

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557952

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=16231289

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ResearchGate publication ID

7535713

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(Q29619767)

Very fast empirical prediction and rationalization of protein pKa values

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