2014
DOI: 10.1021/ja503069k
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Concerted Dihedral Rotations Give Rise to Internal Friction in Unfolded Proteins

Abstract: Protein chains undergo conformational diffusion during folding and dynamics, experiencing both thermal kicks and viscous drag. Recent experiments have shown that the corresponding friction can be separated into wet friction, which is determined by the solvent viscosity, and dry friction, where frictional effects arise due to the interactions within the protein chain. Despite important advances, the molecular origins underlying dry friction in proteins have remained unclear. To address this problem, we studied … Show more

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Cited by 101 publications
(191 citation statements)
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“…In particular the contribution of dihedral rotations to internal friction has been studied in quite some detail recently. 14 The same behavior has been observed before for various molecular systems. For example, Ref.…”
Section: B Viscosity Dependencesupporting
confidence: 82%
See 1 more Smart Citation
“…In particular the contribution of dihedral rotations to internal friction has been studied in quite some detail recently. 14 The same behavior has been observed before for various molecular systems. For example, Ref.…”
Section: B Viscosity Dependencesupporting
confidence: 82%
“…2 Other studies on this topic have measured the viscosity dependence of small ligand dissociation 3,4 or the folding rates of peptides or of entire proteins. [5][6][7][8][9][10][11][12][13][14] Viscosity has an obvious important role in diffusive processes within the cell, but may also have an additional important role in regulating reaction rates and metabolism.…”
Section: Introductionmentioning
confidence: 99%
“…The value of the internal friction time we observe for ubiquitin in 8 M urea at pH 2.5 is similar in magnitude to that of cold shock protein at ∼4 M GdmCl, pH 7 (30) or spectrin domains between 4 and 8 M GdmCl, pH 7 (58). The molecular origin of internal friction in unfolded proteins is currently unclear; simulations have indicated an important role of dihedral angle rotation (61,62), but because internal friction is absent in some proteins at very high denaturant concentrations (30,35), the influence of attractive intrachain interactions (63) and residual structure formation as detected here (Fig. 1) is likely to also contribute.…”
Section: Comparison Of Distances Derived From Single-molecule Fret Andmentioning
confidence: 83%
“…We expect this type of integrated approach to be ideally suited both for reaching a deeper understanding of the role of unfolded state structure and dynamics in protein folding and for linking the conformational and dynamic properties of IDPs to their cellular functions (61,62,85,86).…”
Section: Discussionmentioning
confidence: 99%
“…Subsequently not only these recent experiments [11,12,26] on polypeptides and proteins showed internal friction to play a pivotal role in the dynamics but also motivated theoretical chemical physicists to come up with statistical mechanical models for single polymer chain with the inclusion of internal friction [27][28][29][30][31] and apply these models to investigate the loop formation dynamics. Other than model build up there have been attempts to elucidate the origin of internal friction in proteins based on computer simulation studies [32][33][34][35][36][37][38]. A careful literature survey would reveal that it was de Gennes [39], who introduced the concept of internal viscosity at the single chain level.…”
mentioning
confidence: 99%