Zobrazeno 1 - 10
of 138
pro vyhledávání: '"L, Mehler"'
Publikováno v:
PLoS Computational Biology, Vol 8, Iss 4, p e1002473 (2012)
From computational simulations of a serotonin 2A receptor (5-HT(2A)R) model complexed with pharmacologically and structurally diverse ligands we identify different conformational states and dynamics adopted by the receptor bound to the full agonist 5
Externí odkaz:
https://doaj.org/article/ad94a68747b84125b3b65ad61450d023
Autor:
António M. Baptista, Mats H. M. Olsson, Ernest L. Mehler, Jens Erik Nielsen, Francesca Milletti, Emil Alexov, J. Michael Word, Tommy Carstensen, Jana Shen, Damien Farrell, Yong Huang, Nathan A. Baker, Jim Warwicker, Sarah L. Williams
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:3260-3275
The pK(a) -cooperative aims to provide a forum for experimental and theoretical researchers interested in protein pK(a) values and protein electrostatics in general. The first round of the pK(a) -cooperative, which challenged computational labs to ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91dc26a828c3346049dd12afab87e49f
https://doi.org/10.1002/prot.23189
https://doi.org/10.1002/prot.23189
Autor:
Ernest L. Mehler, Jufang Shan
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:3346-3355
The MM-SCP has been applied to predict pKa values of titratable residues in wild type and mutants of staphylococcal nuclease (SNase). The calculations were based on crystal structures made available by the Garcia-Moreno Laboratory. In the mutants, mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2d5d472482d8e59deb859472cbe072dc
https://doi.org/10.1002/prot.23098
https://doi.org/10.1002/prot.23098
Publikováno v:
Biochemistry. 49:10691-10701
Intracellular loop 2 (IL2) in G-protein-coupled receptors (GPCRs) is functionally important, e.g., in binding to G-protein and β-arrestin. Differences in secondary structure of IL2 in the crystal structures of the very similar β(1)- and β(2)-adren
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e05a1e8edfe7b237788c2ff74c31f82
https://doi.org/10.1021/bi100580s
https://doi.org/10.1021/bi100580s
Autor:
Ernest L. Mehler
Publikováno v:
International Journal of Quantum Chemistry. 14:407-417
The recently proposed self-consistent, nonorthogonal group function approximation has been applied to two interacting, rigid HF molecules in a linear conformation. Wave functions and properties are obtained for a number of orbital groupings and basis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::723da66fbb253d83f9e205507c899a55
https://doi.org/10.1002/qua.560140834
https://doi.org/10.1002/qua.560140834
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 72:646-659
A general method has been developed to characterize the hydrophobicity or hydrophilicity of the microenvironment (MENV), in which a given amino acid side chain is immersed, by calculating a quantitative property descriptor (QPD) based on the relative
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::416e5d5dc0c8a5e1d5e87441a073dac7
https://doi.org/10.1002/prot.21958
https://doi.org/10.1002/prot.21958
Publikováno v:
Journal of Computer-Aided Molecular Design. 20:427-436
A newly developed approach for predicting the structure of segments that connect known elements of secondary structure in proteins has been applied to some of the longer loops in the G-protein coupled receptors (GPCRs) rhodopsin and the dopamine rece
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16f2e4fcaccb53bbefbdd3cb16fd9bde
https://doi.org/10.1007/s10822-006-9056-0
https://doi.org/10.1007/s10822-006-9056-0
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 64:673-690
With the help of the crystal structure of rhodopsin an ab initio method has been developed to calculate the three-dimensional structure of the loops that connect the transmembrane helices (TMHs). The goal of this procedure is to calculate the loop st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7abdce24dcf653903146d7b8966f90d
https://doi.org/10.1002/prot.21022
https://doi.org/10.1002/prot.21022
Autor:
Ernest L. Mehler, Xianfeng Li
Publikováno v:
Cell Biochemistry and Biophysics. 46:123-142
Fibril formation by the Alzheimer's beta-amyloid (Abeta) peptide in brain tissue is integral to the Alzheimer's disease pathology. Understanding the conformational properties and the mechanisms triggering aggregation of the Abeta peptides, at an atom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bdb5da763470c0e815ff272b2d80bdb
https://doi.org/10.1385/cbb:46:2:123
https://doi.org/10.1385/cbb:46:2:123
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 60:464-484
Long dynamics simulations were carried out on the B1 immunoglobulin-binding domain of streptococcal protein G (ProtG) and bovine pancreatic trypsin inhibitor (BPTI) using atomistic descriptions of the proteins and a continuum representation of solven
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::483dfa0c3e129c53ddae416d1f3b7be4
https://doi.org/10.1002/prot.20470
https://doi.org/10.1002/prot.20470