Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Ioannis G. Riziotis"'
Autor:
António J. M. Ribeiro, Ioannis G. Riziotis, Jonathan D. Tyzack, Neera Borkakoti, Janet M. Thornton
Publikováno v:
Biophysical Reviews. 14:1273-1280
Enzyme reactions take place in the active site through a series of catalytic steps, which are collectively termed the enzyme mechanism. The catalytic step is thereby the individual unit to consider for the purposes of building new enzyme mechanisms
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13a83832075e262de30ee1e70b5714f2
https://doi.org/10.1007/s12551-022-01022-9
https://doi.org/10.1007/s12551-022-01022-9
Autor:
Antonio J. M. Ribeiro, Ioannis G. Riziotis, Jonathan D. Tyzack, Neera Borkakoti, Janet M. Thornton
A rich literature dedicated to understanding the reaction mechanisms of hundreds of enzymes has emerged over time from the works of experimental and computational researchers. This body of information can now be the starting point for an entirely nov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::611933cdc7fa6c733a9a5764113dd611
https://doi.org/10.1101/2022.09.05.506575
https://doi.org/10.1101/2022.09.05.506575
Autor:
Janet Thornton, Ioannis G. Riziotis
Publikováno v:
Protein science : a publication of the Protein Society. 31(7)
Structural templates are 3D signatures representing protein functional sites, such as ligand binding cavities, metal coordination motifs, or catalytic sites. Here we explore methods to generate template libraries and algorithms to query structures fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00fddac9bdd5e2e37dedb5e6924b3c7b
https://pubmed.ncbi.nlm.nih.gov/35762726
https://pubmed.ncbi.nlm.nih.gov/35762726
Conformational variation in catalytic residues can be captured as alternative snapshots in enzyme crystal structures. Addressing the question of whether active site flexibility is an intrinsic and essential property of enzymes for catalysis, we prese
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc5ea8621c807d85b2a74ad52aafd6ae
https://doi.org/10.1101/2021.12.12.472283
https://doi.org/10.1101/2021.12.12.472283
Autor:
Eleni Papachristou, Ioannis G. Riziotis, Rigini Papi, Georgios Karolidis, Aglaia Mantsou, Theodora Choli-Papadopoulou, Paraskevas Lamprou
Publikováno v:
ACS biomaterials scienceengineering. 7(11)
Elastin-like polypeptides (ELPs) are protein-based biopolymers genetically produced from polypeptides composed of a repeating pentapeptide sequence V-P-G-X-G. The inherent properties of recombinant ELPs, such as smart nature, controlled sequence comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a70ca8306f2f97e9d6aa1d708ac59ba6
https://pubmed.ncbi.nlm.nih.gov/34666482
https://pubmed.ncbi.nlm.nih.gov/34666482
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 87:966-978
Standard secondary structure elements such as α-helices or β-sheets, are characterized by repeating backbone torsion angles (φ,ψ) at the single residue level. Two-residue motifs of the type (φ,ψ)2 are also observed in nonlinear conformations, m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26d260286328fd127bcee0ba52610006
https://doi.org/10.1002/prot.25758
https://doi.org/10.1002/prot.25758