Zobrazeno 1 - 10
of 74
pro vyhledávání: '"Richard H. Henchman"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
Understanding the intricate interplay of interactions between proteins, excipients, ions and water is important to achieve the effective purification and stable formulation of protein therapeutics. The free energy of lysozyme interacting with two kin
Externí odkaz:
https://doaj.org/article/b0d344dd009f4ad2b2d1a9622f2c7b2f
Publikováno v:
Entropy, Vol 21, Iss 8, p 750 (2019)
Accurately calculating the entropy of liquids is an important goal, given that many processes take place in the liquid phase. Of almost equal importance is understanding the values obtained. However, there are few methods that can calculate the entro
Externí odkaz:
https://doaj.org/article/df14ba20f46b41daab467b783f9e3eb8
Publikováno v:
Journal of Computer-Aided Molecular Design
Free energy drives a wide range of molecular processes such as solvation, binding, chemical reactions and conformational change. Given the central importance of binding, a wide range of methods exist to calculate it, whether based on scoring function
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d9e1c7940ca7cf4c0b06d0291112db4
https://doi.org/10.1007/s10822-021-00406-5
https://doi.org/10.1007/s10822-021-00406-5
Publikováno v:
Journal of Computer-Aided Molecular Design
Falcioni, F, Kalayan, J & Henchman, R 2021, ' Energy-Entropy Prediction of Octanol-Water LogP of SAMPL7 N-Acyl Sulfonamide Bioisosters ', Journal of computer-aided molecular design, vol. 35, no. 7, pp. 831-840 . https://doi.org/10.1007/s10822-021-00401-w
Falcioni, F, Kalayan, J & Henchman, R 2021, ' Energy-Entropy Prediction of Octanol-Water LogP of SAMPL7 N-Acyl Sulfonamide Bioisosters ', Journal of computer-aided molecular design, vol. 35, no. 7, pp. 831-840 . https://doi.org/10.1007/s10822-021-00401-w
Partition coefficients quantify a molecule’s distribution between two immiscible liquid phases. While there are many methods to compute them, there is not yet a method based on the free energy of each system in terms of energy and entropy, where en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8658c6fb79c944250ef707da59009c4
https://doi.org/10.1007/s10822-021-00401-w
https://doi.org/10.1007/s10822-021-00401-w
Publikováno v:
ProteinsREFERENCES.
The total free energy of a hydrated biomolecule and its corresponding decomposition of energy and entropy provides detailed information about regions of thermodynamic stability or instability. The free energies of four hydrated globular proteins with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce74e159ce44be628602bc3fe4a8d674
https://pubmed.ncbi.nlm.nih.gov/35964252
https://pubmed.ncbi.nlm.nih.gov/35964252
Publikováno v:
The Journal of Physical Chemistry A. 125:1720-1737
The viomycin biosynthesis enzyme VioC is a nonheme iron and α-ketoglutarate-dependent dioxygenase involved in the selective hydroxylation of l-arginine at the C3-position for antibiotics biosynthesis. Interestingly, experimental studies showed that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7286ca82c0daf29db9bff0652a01259
https://doi.org/10.1021/acs.jpca.1c00141
https://doi.org/10.1021/acs.jpca.1c00141
Publikováno v:
Kalayan, J, Henchman, R H & Warwicker, J 2019, ' A Model for Counterion Binding and Charge Reversal on Protein Surfaces ', Molecular Pharmaceutics, vol. 17, no. 2, pp. 595-603 . https://doi.org/10.1021/acs.molpharmaceut.9b01047
The structural stability and solubility of proteins in liquid therapeutic formulations is important, especially since new generations of therapeutics are designed for efficacy before consideration of stability. We introduce an electrostatic binding m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73ed519adbb1e720812a0d7a05799723
https://doi.org/10.1021/acs.molpharmaceut.9b01047
https://doi.org/10.1021/acs.molpharmaceut.9b01047
Autor:
Richard H Henchman
Slides for presentation at 16th German Conference on Cheminformatics and SAMPL Satellite Workshop - Virtual Edition, 4 November 2020
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27af4e73d3cc6e5b4c51306f3f108d7b
Publikováno v:
Chakravorty, A, Higham, J & Henchman, R H 2020, ' Entropy of Proteins Using Multiscale Cell Correlation ', Journal of Chemical Information and Modeling . https://doi.org/10.1021/acs.jcim.0c00611
A new multiscale method is presented to calculate the entropy of proteins from molecular dynamics simulations. Termed Multiscale Cell Correlation (MCC), the method decomposes the protein into sets of rigid-body units based on their covalent-bond conn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17d14f3ede251c07c507726deb71d66b
https://pure.manchester.ac.uk/ws/files/176495162/manuscript.pdf
https://pure.manchester.ac.uk/ws/files/176495162/manuscript.pdf
Autor:
Richard H. Henchman, Chandra S. Verma, Aishwary Tukaram Shivgan, Peter J. Bond, Alexander Krah, Roland G. Huber, Paul Matsudaira, Jan K. Marzinek
Publikováno v:
Henchman, R 2020, ' Extending the Martini Coarse-Grained Force Field to N-Glycans ', Journal of Chemical Information and Modeling, vol. 60, no. 8, pp. 3864-3883 . https://doi.org/10.1021/acs.jcim.0c00495
Glycans play a vital role in a large number of cellular processes. Their complex and flexible nature hampers structure-function studies using experimental techniques. Molecular dynamics (MD) simulations can help in understanding dynamic aspects of gl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9488286694b9995fb3a97bbfeccbf9cb
https://doi.org/10.1021/acs.jcim.0c00495
https://doi.org/10.1021/acs.jcim.0c00495