Dynamic Folding Pathway Models of the Trp-Cage Protein
Joint Authors
Source
Issue
Vol. 2013, Issue 2013 (31 Dec. 2013), pp.1-9, 9 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2013-06-24
Country of Publication
Egypt
No. of Pages
9
Main Subjects
Abstract EN
Using action-derived molecular dynamics (ADMD), we study the dynamic folding pathway models of the Trp-cage protein by providing its sequential conformational changes from its initial disordered structure to the final native structure at atomic details.
We find that the numbers of native contacts and native hydrogen bonds are highly correlated, implying that the native structure of Trp-cage is achieved through the concurrent formations of native contacts and native hydrogen bonds.
In early stage, an unfolded state appears with partially formed native contacts (~40%) and native hydrogen bonds (~30%).
Afterward, the folding is initiated by the contact of the side chain of Tyr3 with that of Trp6, together with the formation of the N-terminal α-helix.
Then, the C-terminal polyproline structure docks onto the Trp6 and Tyr3 rings, resulting in the formations of the hydrophobic core of Trp-cage and its near-native state.
Finally, the slow adjustment processes of the near-native states into the native structure are dominant in later stage.
The ADMD results are in agreement with those of the experimental folding studies on Trp-cage and consistent with most of other computational studies.
American Psychological Association (APA)
Lee, In-Ho& Kim, Seung-Yeon. 2013. Dynamic Folding Pathway Models of the Trp-Cage Protein. BioMed Research International،Vol. 2013, no. 2013, pp.1-9.
https://search.emarefa.net/detail/BIM-1005550
Modern Language Association (MLA)
Lee, In-Ho& Kim, Seung-Yeon. Dynamic Folding Pathway Models of the Trp-Cage Protein. BioMed Research International No. 2013 (2013), pp.1-9.
https://search.emarefa.net/detail/BIM-1005550
American Medical Association (AMA)
Lee, In-Ho& Kim, Seung-Yeon. Dynamic Folding Pathway Models of the Trp-Cage Protein. BioMed Research International. 2013. Vol. 2013, no. 2013, pp.1-9.
https://search.emarefa.net/detail/BIM-1005550
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1005550