Calculations of heat of solvation by a simple electrostatic approach to molecular interactions

Autor: H. O. Villar, R. E. Cachau, Eduardo A. Castro

Publikováno v: Chinese Journal of Chemistry. 10:107-116

An extremely simple formula to estimate the heat of formation of complexes between an ion and a polar molecule or between highly polar systems is presented. The formula is entirely electrostatic and the expression used is verified by means of perturb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e263027f70903d4b090ab7122faafd98
https://doi.org/10.1002/cjoc.19920100202

Conformational Space Profiling Enhances Generic Molecular Representation for AI‐Powered Ligand‐Based Drug Discovery.

Autor: Wang, Lin¹ (AUTHOR), Wang, Shihang¹ (AUTHOR), Yang, Hao¹ (AUTHOR), Li, Shiwei¹ (AUTHOR), Wang, Xinyu¹ (AUTHOR), Zhou, Yongqi¹ (AUTHOR), Tian, Siyuan¹ (AUTHOR), Liu, Lu¹ (AUTHOR), Bai, Fang² (AUTHOR) baifang@shanghaitech.edu.cn

Publikováno v: Advanced Science. 10/28/2024, Vol. 11 Issue 40, p1-14. 14p.

A new addition to the structural bioinformatics toolbox: 3D models of short bioactive peptides from multiple sequences using feedback restrained molecular dynamics (FRMD)

Autor: R E, Cachau, G, González-Sapienza, S K, Burt, O N, Ventura

Publikováno v: Cellular and molecular biology (Noisy-le-Grand, France). 49(6)

Modem molecular biology techniques allow the use of new approaches for the 3D mapping of 1D information. Molecular biology techniques are capable of producing large amounts of 1D information (sequences) from a number of different sources (phage displ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::77afaff3f20ca9a67c44a75b531a2555
https://pubmed.ncbi.nlm.nih.gov/14656056

A quantum mechanical model of the hydration and acidity of the active site in aspartic proteases

Autor: I A, Topol, R E, Cachau, S K, Burt, J W, Erickson

Publikováno v: Advances in experimental medicine and biology. 362

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::91afed96df8d946210fd968635ec890b
https://pubmed.ncbi.nlm.nih.gov/8540370

Extracting binding energies and binding modes from biomolecular simulations of fragment binding to endothiapepsin.

Autor: Schmitz B; Institute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany., Frieg B; Institute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.; John von Neumann Institute for Computing (NIC), Jülich Supercomputing Centre (JSC), and Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany., Homeyer N; Institute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany., Jessen G; Institute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany., Gohlke H; Institute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.; John von Neumann Institute for Computing (NIC), Jülich Supercomputing Centre (JSC), and Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.; Institute of Bio- and Geosciences (IBG-4: Bioinformatics), Forschungszentrum Jülich, Jülich, Germany.

Publikováno v: Archiv der Pharmazie [Arch Pharm (Weinheim)] 2024 May; Vol. 357 (5), pp. e2300612. Date of Electronic Publication: 2024 Feb 06.