Fast folding and slow unfolding of a resurrected Precambrian protein
Author:
Funder
Junta de Andalucia
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference10 articles.
1. Evidence for the principle of minimal frustration in the evolution of protein folding landscapes
2. Single-molecule paleoenzymology probes the chemistry of resurrected enzymes
3. Conservation of Protein Structure over Four Billion Years
4. Mutational Studies on Resurrected Ancestral Proteins Reveal Conservation of Site-Specific Amino Acid Preferences throughout Evolutionary History
5. Selection for Protein Kinetic Stability Connects Denaturation Temperatures to Organismal Temperatures and Provides Clues to Archaean Life
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