TY - GEN
T1 - Mechanical characterization of prion fibrils using coarse-grained modeling approach in Silico
AU - Yoon, Gwonchan
AU - Kim, Young Kab
AU - Eom, Kilho
AU - Na, Sungsoo
PY - 2012
Y1 - 2012
N2 - Prions are self-replicating proteins composed of β-sheet secondary structures that can cause neurodegenerative disorders such as Bovine Spongiform Encephalopathy(also known as mad cow disease), and they also can be found in various kinds of disease such as Alzheimer's diseases and type II diabetes [1]. At the molecular level, prions propagate an amyloid fibril by forming β-sheet structures that are oriented perpendicularly to the fibril axis, and connected through a dense hydrogen-bonding network which makes them stable [1]. Because of the mechanical toughness, understanding the mechanical characteristics of prion protein could play a key role to the development of the pathological treatment for those diseases caused by prion. One of the well-known prion proteins is HET-s protein which appears to have specific biological function in the filamentous fungus Podospora anserine. In this study, we elongated the HET-s(218-289) and characterized the mechanical properties of HET-s. Normal Mode Analysis(NMA) with Elastic Network Model(ENM) are used to predict the possible elastic deformation mode of the HET-s(218-289). ANM(Anisotropic Network Model) and continuous beam model are also used to make the result.
AB - Prions are self-replicating proteins composed of β-sheet secondary structures that can cause neurodegenerative disorders such as Bovine Spongiform Encephalopathy(also known as mad cow disease), and they also can be found in various kinds of disease such as Alzheimer's diseases and type II diabetes [1]. At the molecular level, prions propagate an amyloid fibril by forming β-sheet structures that are oriented perpendicularly to the fibril axis, and connected through a dense hydrogen-bonding network which makes them stable [1]. Because of the mechanical toughness, understanding the mechanical characteristics of prion protein could play a key role to the development of the pathological treatment for those diseases caused by prion. One of the well-known prion proteins is HET-s protein which appears to have specific biological function in the filamentous fungus Podospora anserine. In this study, we elongated the HET-s(218-289) and characterized the mechanical properties of HET-s. Normal Mode Analysis(NMA) with Elastic Network Model(ENM) are used to predict the possible elastic deformation mode of the HET-s(218-289). ANM(Anisotropic Network Model) and continuous beam model are also used to make the result.
KW - Coarse-grained model
KW - Elastic network model
KW - Euler-Bernoulli beam theory
KW - Mechanical characterization
KW - Normal mode analysis
KW - Prion
UR - http://www.scopus.com/inward/record.url?scp=84864986364&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84864986364&partnerID=8YFLogxK
M3 - Conference contribution
AN - SCOPUS:84864986364
SN - 9781466562769
T3 - Technical Proceedings of the 2012 NSTI Nanotechnology Conference and Expo, NSTI-Nanotech 2012
SP - 102
EP - 105
BT - Technical Proceedings of the 2012 NSTI Nanotechnology Conference and Expo, NSTI-Nanotech 2012
T2 - Nanotechnology 2012: Bio Sensors, Instruments, Medical, Environment and Energy - 2012 NSTI Nanotechnology Conference and Expo, NSTI-Nanotech 2012
Y2 - 18 June 2012 through 21 June 2012
ER -