1996
DOI: 10.1038/nsb0196-54
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Amino-acid substitutions in a surface turn modulate protein stability

Abstract: A surface turn position in a four-helix bundle protein, Rop, was selected to investigate the role of turns in protein structure and stability. Although all twenty amino acids can be substituted at this position to generate a correctly folded protein, they produce an unusually large range of thermodynamic stabilities. Moreover, the majority of substitutions give rise to proteins with enhanced thermal stability compared to that of the wild type. By introducing the same twenty mutations at this position, but in a… Show more

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Cited by 100 publications
(84 citation statements)
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“…65 Also, insertion of Gly residues into this loop have been shown to be entropically destabilizing relative to the natural sequence by 0.5-1.0 kcal mol −1 for each Gly residue inserted. 66 Thus, a welldesigned loop can stabilize a protein by several kilocalories per mole relative to a randomly chosen or poorly designed sequence.…”
Section: Determinants Of the Free Energy Gapmentioning
confidence: 99%
“…65 Also, insertion of Gly residues into this loop have been shown to be entropically destabilizing relative to the natural sequence by 0.5-1.0 kcal mol −1 for each Gly residue inserted. 66 Thus, a welldesigned loop can stabilize a protein by several kilocalories per mole relative to a randomly chosen or poorly designed sequence.…”
Section: Determinants Of the Free Energy Gapmentioning
confidence: 99%
“…On the other hand, however, when protein stability is under constant selective pressure, for example for proteins in thermophiles, many small stabilizing variations are accumulated to improve the overall stability (Argos et al, 1979). However, the important contribution of surface residues to protein stability and function (Predki et al, 1996;D.D. Axe & A.R.F., unpublished data) is heavily masked by their high variability.…”
Section: Mutations At the Protein Surfacementioning
confidence: 99%
“…17 Extensive mutations have been made to the core and loop of Rop to probe their effects on stability, folding and structure. 8,[18][19][20][21][22] Recently, we have reported in vivo and in vitro screens for the folding and stability of Rop, with the goal of correlating the effects of many kinds of mutations with changes in thermodynamics. 23,24 A proofof-principle library of mutations in the central core of Rop (I15 T19 L41 A45 to all amino acids with the NNK residue) produced a library of active variants with a range of physical properties (TJM and Lynne Regan, manuscript in preparation).…”
Section: Introductionmentioning
confidence: 99%