2015
DOI: 10.1039/c4cp03058c
|View full text |Cite
|
Sign up to set email alerts
|

The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone

Abstract: Although protein folding is often described by motion on a funnel-shaped overall topology of the energy landscape, the many local interactions that can occur result in considerable landscape roughness which slows folding by increasing internal friction. Recent experimental results have brought to light that this roughness also causes unusual diffusional behaviour of the backbone of an unfolded protein, i.e. the relative motion of protein sections cannot be described by the normal diffusion equation, but shows … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

2
26
0

Year Published

2016
2016
2020
2020

Publication Types

Select...
7

Relationship

0
7

Authors

Journals

citations
Cited by 26 publications
(28 citation statements)
references
References 208 publications
(426 reference statements)
2
26
0
Order By: Relevance
“…According to Eq. 4 (see Materials and Methods section), the effect of urea on k f mainly originates from the change of energy barrier (activation energy ), because the changes of viscosity and internal friction at low concentration of urea buffer (0.25 M) are negligible ( ) 35 , 36 . Therefore, the change of activation energy is given by, …”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…According to Eq. 4 (see Materials and Methods section), the effect of urea on k f mainly originates from the change of energy barrier (activation energy ), because the changes of viscosity and internal friction at low concentration of urea buffer (0.25 M) are negligible ( ) 35 , 36 . Therefore, the change of activation energy is given by, …”
Section: Resultsmentioning
confidence: 99%
“…The folding rate ( k f ) is related to the activation energy ( ) by 41 , 42 where C is the frequency factor for the folding process, σ refers to the “internal friction”, and η is the viscosity of solvent. σ reflects the contribution of the energy landscape ruggedness to the reaction rate and is dominated by the structure of a protein when denaturant concentrations are low 36 .…”
Section: Methodsmentioning
confidence: 99%
“…Therefore, temperature dependence of conformational motion is related to the peptide's conformational free energy landscape [43][44][45] . For peptides and proteins, this energy landscape is rough, populated by small kinetic traps [46][47][48][49] . As the peptide diffuses through its conformations, it must hop between these traps.…”
mentioning
confidence: 99%
“…In fact, the roughness of the potential is crucial in biophysical contexts such as in protein folding [19,20], where the potential surface can exhibit a rich structure of maxima and minima, hierarchical or not. The roughness in energy landscapes has been experimentally measured in proteins [21][22][23][24] * Electronic address: sabrina.mga@gmail.com † Electronic address: celia.fis@puc-rio.br but can also be microfabricated, for instance, holographic optical tweezers, used in optical ratchets, can generate complicated potential energy landscapes for Brownian particles [25].…”
Section: Introductionmentioning
confidence: 99%