Structural determinants of the rate of protein folding

DOI10.1016/S0022-5193(03)00091-2MaRDI QIDQ2177284zbMATH OpenOpenAlexWikidataFDO

Authors Bengt Nölting, Wolfram Schälike, Patrick Hampel, Florian Grundig, Siegfried Gantert, Nicole Sips, Wolfhard Bandlow, Phoebe X. Qi

Publication date 6 May 2020

Published in Journal of Theoretical Biology (Search for Journal in Brave)

Full work available at URL https://doi.org/10.1016/s0022-5193(03)00091-2

zbMATH Keywords

helix-coil transition\(\Phi\)-value analysischain topologynucleation-condensation mechanismprotein folding kineticsrational design of enzymes

Mathematics Subject Classification ID

Protein sequences, DNA sequences (92D20) Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45)

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• Folding degrees of azurins and pseudoazurins: Implications for structure and function
• Exploring the correlation between the folding rates of proteins and the entanglement of their native states
• Influence of conformational entropy on the protein folding rate
• Global and local prediction of protein folding rates based on sequence autocorrelation information

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