Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Seyedeh Maryam Salehi"'
Publikováno v:
CHIMIA, Vol 77, Iss 11 (2023)
Through a lens encompassing KNIME workflows, QSAR models, LLMs, and chemical substructure search strategies, the article navigates the essential considerations driving innovation and progress in industrial cheminformatics for medicinal chemistry and
Externí odkaz:
https://doaj.org/article/33e44f2e81e6435fb8ae9540d1f4bd58
Autor:
Seyedeh Maryam Salehi, Markus Meuwly
Publikováno v:
Molecules, Vol 27, Iss 3, p 839 (2022)
The changes in the local and global dynamics of azide-labelled lysozyme compared with that of the wild type protein are quantitatively assessed for all alanine residues along the polypeptide chain. Although attaching -N3 to alanine residues has been
Externí odkaz:
https://doaj.org/article/bcce70a1cf954f3abf9472bc6e24766e
Autor:
Meuwly, Seyedeh Maryam Salehi, Markus
Publikováno v:
Molecules; Volume 27; Issue 3; Pages: 839
The changes in the local and global dynamics of azide-labelled lysozyme compared with that of the wild type protein are quantitatively assessed for all alanine residues along the polypeptide chain. Although attaching -N3 to alanine residues has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=multidiscipl::8b4865fbe74882bff3ba1ac0fd6ec08d
Autor:
Kai Töpfer, Andrea Pasti, Anuradha Das, Seyedeh Maryam Salehi, Luis Itza Vazquez-Salazar, David Rohrbach, Thomas Feurer, Peter Hamm, Markus Meuwly
The spectroscopy and structural dynamics of a deep eutectic mixture (KSCN/acetamide) with varying water content is investigated from 2D IR (with the C-N stretch vibration of the SCN$^-$ anions as the reporter) and THz spectroscopy. Molecular dynamics
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d8796fb11946bf03d7da6c709a6a028
Autor:
Markus Meuwly, Seyedeh Maryam Salehi
Azido-modified alanine residues (AlaN$_3$) are environment-sensitive, minimally invasive infrared probes for the site-specific investigation of protein structure and dynamics. Here, the capability of the label is investigated to query whether or not
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83e43b23c1291a6979470a944fe9c8d8
Autor:
Seyedeh Maryam Salehi, Markus Meuwly
Publikováno v:
Molecules, Vol 27, Iss 839, p 839 (2022)
The changes in the local and global dynamics of azide-labelled lysozyme compared with that of the wild type protein are quantitatively assessed for all alanine residues along the polypeptide chain. Although attaching -N3 to alanine residues has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d1af3f903512c748845ed6c9571cbd4
http://arxiv.org/abs/2112.00606
http://arxiv.org/abs/2112.00606
Publikováno v:
The Journal of Chemical Physics. 158:025101
The local hydration around tetrameric hemoglobin (Hb) in its T0 and R4 conformational substates is analyzed based on molecular dynamics simulations. Analysis of the local hydrophobicity (LH) for all residues at the α1 β2 and α2 β1 interfaces, res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3e1240413ccf057503acd4f48ca0a427
https://doi.org/10.1063/5.0129990
https://doi.org/10.1063/5.0129990
Autor:
Seyedeh Maryam Salehi, Markus Meuwly
The spectroscopic response of and structural dynamics around all azido-modified alanine residues (AlaN$_3$) in Lysozyme is characterized. It is found that AlaN$_3$ is a positionally sensitive probe for the local dynamics, covering a frequency range o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4e7273d6b4caffcbfd5df0e465b07f8
http://arxiv.org/abs/2102.06545
http://arxiv.org/abs/2102.06545
Publikováno v:
The journal of physical chemistry. B. 123(15)
Azido-derivatized amino acids are potentially useful, positionally resolved spectroscopic probes for studying the structural dynamics of proteins and macromolecules in solution. To this end, a computational model for the vibrational modes of N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::739cb13d42af84badd79d81bdc0594fa
https://pubmed.ncbi.nlm.nih.gov/30830786
https://pubmed.ncbi.nlm.nih.gov/30830786
Publikováno v:
The Journal of Chemical Physics. 153:010901
Extensions and improvements of empirical force fields are discussed in view of applications to computational vibrational spectroscopy and reactive molecular dynamics simulations. Particular focus is on quantitative studies, which make contact with ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3729d32cc38c9db530eea786727067f
https://doi.org/10.1063/5.0009628
https://doi.org/10.1063/5.0009628