Protein stabilization by hydrophobic interactions at the surface

Burg, Bertus van den; Dijkstra, Bauke W.; Vriend, Gert; Vinne, Bernard van der; Venema, Gerard; Eijsink, Vincent G. H.

doi:10.1111/j.1432-1033.1994.tb18702.x

Cited by 103 publications

(28 citation statements)

References 41 publications

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“…Both Arg and Lys are also capable to do so through their long aliphatic moieties. 26 The presence of other residues at this position resulted in partial/total loss of recognition. The above described effects were specific, since almost all the mutated variants were well recognized by cetuximab (Fig.…”

Section: Both the Target Antigenic Region And The Nimotuzumab Paratopmentioning

confidence: 99%

Delineating the functional map of the interaction between nimotuzumab and the epidermal growth factor receptor

Tundidor

García-Hernández

Pupo

et al. 2014

mAbs

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Section: Both the Target Antigenic Region And The Nimotuzumab Paratopmentioning

confidence: 99%

Delineating the functional map of the interaction between nimotuzumab and the epidermal growth factor receptor

Tundidor

García-Hernández

Pupo

et al. 2014

mAbs

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“…[1][2][3][4][5][6][7][8][9][10] Generally, HIs are less directional and smaller in magnitude than other noncovalent interactions (NCIs)-like Hbonding or salt bridges. [1][2][3][4][5][6][7][8][9][10] Generally, HIs are less directional and smaller in magnitude than other noncovalent interactions (NCIs)-like Hbonding or salt bridges.…”

Section: Introductionmentioning

confidence: 99%

Assessment of hydrophobic interactions and their contributions through the analysis of the methane dimer

2014

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Hydrophobic Interactions (HIs) are important in many phenomena of molecular recognition in chemistry and biology. Still, the relevance of HIs is sometimes difficult to evaluate particularly in large systems and intramolecular interactions. We put forward a method to estimate the magnitude and the different contributions of a given HI of the C···C, H-C···H, and H···H type through (i) the analysis of the electron density in the intermolecular region for eleven relative orientations of the methane dimer and (ii) the subsequent decomposition of the corresponding interaction energy in physically significant contributions using Symmetry Adapted Perturbation Theory (SAPT). Strong correlations were found between the topological properties of ρ(r) calculated at intermolecular bond critical points and Eint(SAPT) plus its different contributions with the C···C distance of the considered orientations of (CH4 )2 . These correlations were used to construct Mollier-like diagrams of Eint(SAPT) and its components as a function of the separation between two carbons and the orientation of the groups bonded to these atoms. The ethane dimer and tert-butylcyclohexane are used as representative examples of this new approach. Overall, we anticipate that this new method might prove useful in the study of both intramolecular and intermolecular HIs particularly of those within large systems wherein SAPT or electronic structure calculations are computationally expensive or even prohibitive.

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“…The slope of the thermal denaturation curve for V1L was steeper than that of R-BSX and the rest of the mutants, which suggests that V1L shows better co-operativity in its unfolding pathway. It also indicates that regions of the protein that were previously flexible in the folded protein have now become stable due to the substitution of Leu at that position [17], [18], [19].…”

Section: Discussionmentioning

confidence: 99%

The Critical Role of Partially Exposed N-Terminal Valine Residue in Stabilizing GH10 Xylanase from Bacillus sp.NG-27 under Poly-Extreme Conditions

et al. 2008

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BackgroundUnderstanding the mechanisms that govern protein stability under poly-extreme conditions continues to be a major challenge. Xylanase (BSX) from Bacillus sp. NG-27, which has a TIM-barrel structure, shows optimum activity at high temperature and alkaline pH, and is resistant to denaturation by SDS and degradation by proteinase K. A comparative circular dichroism analysis was performed on native BSX and a recombinant BSX (R-BSX) with just one additional methionine resulting from the start codon. The results of this analysis revealed the role of the partially exposed N-terminus in the unfolding of BSX in response to an increase in temperature.MethodologyWe investigated the poly-extremophilicity of BSX to deduce the structural features responsible for its stability under one set of conditions, in order to gain information about its stability in other extreme conditions. To systematically address the role of the partially exposed N-terminus in BSX stability, a series of mutants was generated in which the first hydrophobic residue, valine (Val1), was either deleted or substituted with various amino acids. Each mutant was subsequently analyzed for its thermal, SDS and proteinase K stability in comparison to native BSX.ConclusionsA single conversion of Val1 to glycine (Gly) changed R-BSX from being thermo- and alkali- stable and proteinase K and SDS resistant, to being thermolabile and proteinase K-, alkali- and SDS- sensitive. This result provided insight into the structure-function relationships of BSX under poly-extreme conditions. Molecular, biochemical and structural data revealed that the poly-extremophilicity of BSX is governed by a partially exposed N-terminus through hydrophobic interactions. Such hitherto unidentified N-terminal hydrophobic interactions may play a similar role in other proteins, especially those with TIM-barrel structures. The results of the present study are therefore of major significance for protein folding and protein engineering.

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Protein stabilization by hydrophobic interactions at the surface

Cited by 103 publications

References 41 publications

Delineating the functional map of the interaction between nimotuzumab and the epidermal growth factor receptor

Delineating the functional map of the interaction between nimotuzumab and the epidermal growth factor receptor

Assessment of hydrophobic interactions and their contributions through the analysis of the methane dimer

The Critical Role of Partially Exposed N-Terminal Valine Residue in Stabilizing GH10 Xylanase from Bacillus sp.NG-27 under Poly-Extreme Conditions

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