Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Shiyang Long"'
Publikováno v:
IEEE Access, Vol 11, Pp 121882-121891 (2023)
Automatic 2D vision-based defect detection on sealing nail (SealN) surfaces is challenging due to interference of complex backgrounds with non-homogeneous and low contrast between foreground and background. Inspired by an interesting observation that
Externí odkaz:
https://doaj.org/article/8fd62111d53640e9991bd982f12ac2be
Publikováno v:
PLoS ONE, Vol 10, Iss 6, p e0129846 (2015)
Hierarchical organization of free energy landscape (FEL) for native globular proteins has been widely accepted by the biophysics community. However, FEL of native proteins is usually projected onto one or a few dimensions. Here we generated collectiv
Externí odkaz:
https://doaj.org/article/2537b9ed4f77418ebcb869f8a81ed429
Publikováno v:
RSC Advances. 9:13949-13958
The free energy landscape (FEL) of a given complex molecular system is fundamentally the joint probability density of its many comprising degrees of freedom (DOFs). Computation of a complete FEL at atomistic scale is unfortunately intractable for a t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::752d26e2fd2f3ce7affc1a66beac1b00
https://doi.org/10.1039/c9ra02191d
https://doi.org/10.1039/c9ra02191d
Autor:
Shiyang Long, Pu Tian
Publikováno v:
RSC Advances. 9:38391-38396
Protein secondary structure (SS) prediction is important for studying protein structure and function. Both traditional machine learning methods and deep learning neural networks have been utilized and great progress has been achieved in approaching t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1d40192093f5b0fcf8b00612e947901
https://doi.org/10.1039/c9ra05218f
https://doi.org/10.1039/c9ra05218f
Autor:
Shiyang Long, Pu Tian
Rapid and accurate assessment of protein structural models is essential for protein structure prediction and design. Great progress has been made in this regard, especially by recent development of ``knowledge-based'' potentials. Various machine lear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1139a7710bb23b7d094efc24d45f0e4
http://arxiv.org/abs/1907.04914
http://arxiv.org/abs/1907.04914
Autor:
Shiyang Long, Pu Tian
Publikováno v:
Scientific Reports
Protein allostery requires dynamical structural correlations. Physical origin of which, however, remain elusive despite intensive studies during last two decades. Based on analysis of molecular dynamics (MD) simulation trajectories for ten proteins w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93d47420f0a416a52211946a97268502
Publikováno v:
Journal of molecular modeling. 22(8)
Cytosolic sulfotransferases (SULTs) catalyze the transfer of a sulfonate group from the unique cofactor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to a large number of diverse substrates. In this work, tunnels that facilitate the transport of subst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b565f2f8cdb562ea6cea731e025d2235
https://pubmed.ncbi.nlm.nih.gov/27392745
https://pubmed.ncbi.nlm.nih.gov/27392745
Publikováno v:
Scientific Reports
Trajectories provide dynamical information that is discarded in free energy calculations, for which we sought to design a scheme with the hope of saving cost for generating dynamical information. We first demonstrated that snapshots in a converged tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0027e2a1aadfe57d966657683ba1b35
http://arxiv.org/abs/1505.04655
http://arxiv.org/abs/1505.04655
Publikováno v:
Journal of molecular modeling. 21(8)
Sulfotransferases catalyze transfer of the sulfuryl-group (-SO3) from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to a large number of substrates. They play an important role in phase II metabolic process. The impact of the cofactor (PAPS) on the st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61db35a0715db0be8c9cb2e90ed47107
https://pubmed.ncbi.nlm.nih.gov/26149755
https://pubmed.ncbi.nlm.nih.gov/26149755