Relative importance of secondary structure and solvent accessibility to the stability of protein mutants. A case study with amino acid properties and energetics on T4 and human lysozymes

DOI10.1016/J.COMPBIOLCHEM.2004.12.002MaRDI QIDQ2500258zbMATH OpenOpenAlexWikidataFDO

Authors K. Saraboji, M. Michael Gromiha, M. N. Ponnuswamy

Publication date 23 August 2006

Published in Computational Biology and Chemistry (Search for Journal in Brave)

Full work available at URL https://doi.org/10.1016/j.compbiolchem.2004.12.002

zbMATH Keywords

Protein stabilityFree energyAmino acid propertiesMultiple regression analysisProtein mutants

Mathematics Subject Classification ID

Biochemistry, molecular biology (92C40)

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(6)

• Knowledge acquisition and development of accurate rules for predicting protein stability changes
• Analyzing effects of naturally occurring missense mutations
• Prediction of the determinants of thermal stability by linear discriminant analysis: the case of the glutamate dehydrogenase protein family
• Structural role of exon-coded fragment of polypeptide chains in selected enzymes
• Metadynamics study of mutant human interferon-gamma forms
• Molecular dynamics simulations study of influence of Tyr422Ala mutation on transcriptional enhancer activation domain 4 (TEAD4) and transcription co-activators complexes

Describes a project that uses

Uses Software

• Naccess
• ProTherm

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