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Can Contact Potentials Reliably Predict Stability of Proteins?
Jainab Khatun
, Sagar D. Khare
, Nikolay V. Dokholyan
Cancer Institute, Next-Generation Therapies
Penn State Cancer Institute
Penn State Neuroscience Institute
Penn State Clinical and Translational Science Institute (CTSI)
Center for Cannabis and Natural Product Pharmaceuticals (CCNPP)
Department of Neuroscience and Experimental Therapeutics
Research output
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Contribution to journal
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Article
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peer-review
64
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Scopus citations
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Keyphrases
Contact Potential
100%
Protein Stability
100%
Contact Parameters
50%
Protein Family
33%
Interaction Potential
16%
Amino Acid Residues
16%
Contact Interaction
16%
Protein Folding
16%
Reliability Prediction
16%
Effective Free Energy
16%
Single Cell Protein
16%
Interaction Model
16%
Solvation
16%
In Silico
16%
Prediction Accuracy
16%
Change of Measure
16%
Free Energy
16%
Interaction Parameter
16%
Contact Model
16%
Amino Acid Position
16%
G-value
16%
Statistical Test
16%
Stability Change
16%
Protein Engineering
16%
Correlation between Parameters
16%
Protein Conformation
16%
Amino Acid Interactions
16%
Protein Thermal Stability
16%
Experimental Accuracy
16%
Biochemistry, Genetics and Molecular Biology
Amino Acids
100%
Protein Family
66%
Conformation
33%
Protein Folding
33%
Solvation
33%
Protein Engineering
33%
Protein Conformation
33%
Statistical Test
33%
Food Science
Amino Acid
100%
Protein Folding
33%
Protein Conformation
33%