Smooth Change, Mechanistic Fluctuation: Thermodynamic System Drift in Protein Evolution
نویسندگان
چکیده
منابع مشابه
Smooth Change, Mechanistic Fluctuation: Thermodynamic System Drift in Protein Evolution
If you heat a protein up, the tertiary contacts that secure its three-dimensional shape weaken until eventually the protein unfolds, or ‘‘melts.’’ Not surprisingly, proteins from thermophilic organisms, such as the bacteria that live in hot springs, tend to have higher melting temperatures than their homologs from mesophiles like humans or the bacteria that live within them. The increased melti...
متن کاملThermodynamic System Drift in Protein Evolution
Proteins from thermophiles are generally more thermostable than their mesophilic homologs, but little is known about the evolutionary process driving these differences. Here we attempt to understand how the diverse thermostabilities of bacterial ribonuclease H1 (RNH) proteins evolved. RNH proteins from Thermus thermophilus (ttRNH) and Escherichia coli (ecRNH) share similar structures but differ...
متن کاملCorrection: Thermodynamic System Drift in Protein Evolution
At the time of publication, the ancestral sequence data from this paper had not been deposited. The ancestral sequences shown in S2B Fig. are now available in GenBank (KP271037—KP271043). An easily accessible sequence alignment file for S2B Fig. is now also available (S1 File). an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestri...
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The relationships among reversible Carnot cycles, the absence of perpetual motion machines, and the existence of a nondecreasing globally unique entropy function form the starting point of many textbook presentations of the foundations of thermodynamics. However, the thermal fluctuation phenomena associated with statistical mechanics has been argued to restrict the domain of validity of this ba...
متن کاملStructural drift: a possible path to protein fold change
SUMMARY Along with their mutating sequences, protein structures change in time. Analyzing a formate dehydrogenase domain that is evolutionarily related to ferredoxin, but simultaneously contains all the structural elements of a beta-Grasp fold, we illustrate here a mechanism termed as structural drift, by which changes to a protein fold can occur. CONTACT [email protected].
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ژورنال
عنوان ژورنال: PLoS Biology
سال: 2014
ISSN: 1545-7885
DOI: 10.1371/journal.pbio.1001992