Thermal stability and protein structure

Amino acid sequences have been compared for thermophilic and mesophilic molecules of ferredoxin, glyceraldehyde-3-phosphate dehydrogenase, and lactate dehydrogenase. It is shown that Gly, Ser, Ser, Lys, and Asp in mesophiles are generally substituted by Ala, Ala, Thr, Arg, and Glu, respectively, in...

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Bibliographic Details
Published in:Biochemistry (Easton) 1979-12, Vol.18 (25), p.5698-5703
Main Authors: Argos, Patrick, Rossmann, Michael G, Grau, Ulrich M, Zuber, Herbert, Frank, Gerhard, Tratschin, Jon Duri
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Bacteria - analysis
Drug Stability
Ferredoxins
Glyceraldehyde-3-Phosphate Dehydrogenases
Isoenzymes
L-Lactate Dehydrogenase
Protein Conformation
Proteins
Species Specificity
Temperature
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Summary:Amino acid sequences have been compared for thermophilic and mesophilic molecules of ferredoxin, glyceraldehyde-3-phosphate dehydrogenase, and lactate dehydrogenase. It is shown that Gly, Ser, Ser, Lys, and Asp in mesophiles are generally substituted by Ala, Ala, Thr, Arg, and Glu, respectively, in thermophiles. These exchanges suggest that thermal stability can be achieved by the addition of many small changes throughout the molecule without significant change in the backbone conformation. Their overall effect is primarily to increase internal and decrease external hydrophobicity as well as to favor helix stabilizing residues in helices. These substitutions minimize interruption of function or internal residue packing arrangements. Although the analysis has been confined to the above-mentioned molecules, the observed stabilizing principles may be more generally applicable.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00592a028