about
Biophysical characterization and mutational analysis of the antibiotic resistance protein NimA from Deinococcus radioduransThermodynamics and structure of a salmon cold active goose-type lysozymeCrystal Structure of the Mobile Metallo- -Lactamase AIM-1 from Pseudomonas aeruginosa: Insights into Antibiotic Binding and the Role of Gln157Synthetic cationic antimicrobial peptides bind with their hydrophobic parts to drug site II of human serum albuminEntropy and Enzyme Catalysis.Ligand binding affinities from MD simulations.The primary structure and specificity determining residues displayed by recombinant salmon antibody domains.Binding affinity prediction with different force fields: examination of the linear interaction energy method.Antimicrobial peptides with stability toward tryptic degradation.Altered activity and physicochemical properties of short cationic antimicrobial peptides by incorporation of arginine analogues.Protein surface softness is the origin of enzyme cold-adaptation of trypsin.Free energy calculations and ligand binding.Computational analysis of binding of P1 variants to trypsin.Anticancer potency of small linear and cyclic tetrapeptides and pharmacokinetic investigations of peptide binding to human serum albumin.Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid.Synthesis of anticancer heptapeptides containing a unique lipophilic β(2,2) -amino acid building block.Computer Simulations Reveal Substrate Specificity of Glycosidic Bond Cleavage in Native and Mutant Human Purine Nucleoside Phosphorylase.Qgui: A high-throughput interface for automated setup and analysis of free energy calculations and empirical valence bond simulations in biological systems.Resolving the energy paradox of chaperone/usher-mediated fibre assembly.Probing the effect of point mutations at protein-protein interfaces with free energy calculationsUnnatural amino acid side chains as S1, S1', and S2' probes yield cationic antimicrobial peptides with stability toward chymotryptic degradation.Electrostatic interactions play an essential role in DNA repair and cold-adaptation of uracil DNA glycosylase.Electrostatic effects play a central role in cold adaptation of trypsin.Structural evidence for lack of inhibition of fish goose-type lysozymes by a bacterial inhibitor of lysozyme.Short cationic antimicrobial peptides bind to human alpha-1 acid glycoprotein with no implications for the in vitro bioactivity.Increased flexibility as a strategy for cold adaptation: a comparative molecular dynamics study of cold- and warm-active uracil DNA glycosylase.Predicting proteinase specificities from free energy calculations.Inspection of the binding sites of proteinase3 for the design of a highly specific substrate.Thermodynamics of the Purine Nucleoside Phosphorylase Reaction Revealed by Computer Simulations.A polarizable embedding DFT study of one-photon absorption in fluorescent proteins.Stem cell regulation: Implications when differentiated cells regulate symmetric stem cell division.Electrostatics of mesophilic and psychrophilic trypsin isoenzymes: qualitative evaluation of electrostatic differences at the substrate binding site.Evaluation of protein-protein association energies by free energy perturbation calculations.Ferric uptake regulator protein: binding free energy calculations and per-residue free energy decomposition.Comparative Molecular Dynamics of Mesophilic and Psychrophilic Protein Homologues Studied by 1.2 ns SimulationsNear Native-State Conformational Landscape of Psychrophilic and Mesophilic Enzymes: Probing the Folding Funnel ModelIon pairs and their role in modulating stability of cold- and warm-active uracil DNA glycosylaseOptimization of electrostatics as a strategy for cold-adaptation: A case study of cold- and warm-active elastasesComparative unfolding studies of psychrophilic and mesophilic uracil DNA glycosylase: MD simulations show reduced thermal stability of the cold-adapted enzymeAlbumin binding of short cationic antimicrobial micropeptides and its influence on the in vitro bactericidal effect
P50
Q27659128-9ECBF679-28E7-4028-9633-BA8C1C6707DAQ27660573-6E90F556-43CB-418E-8461-7526480B0918Q27679496-CFC0CF8B-B7F8-4033-8E75-B8AE864C606AQ27681441-AB364D7F-0F3B-44AC-B70A-8A51D806B925Q30398322-A2C64A2B-F089-409C-A99E-A93C97B72092Q31080599-F82EE730-F959-4799-AFD9-67181CE37220Q33201288-3726B5ED-4E89-4F89-9C8F-A87BC5A18D2EQ33202843-F05937CE-2A5E-41D9-A880-A141648D4378Q33321659-A5CDB3BF-161D-4971-96E3-9A6862B47E82Q33426045-5375A471-CA59-46E7-9ABA-446479F2FBABQ35233581-CE67FB70-8E9E-444D-8AB4-C56C5C47AD68Q35590736-D73A6A6E-89E2-4229-B6EC-865D0474995CQ38272484-B1F1FEBC-3D2F-4C83-A65E-CA7ACACF74E1Q39010669-479A9850-F0DD-4DE4-B895-0FB9036C8756Q39288451-3012E900-C308-43EE-8C83-A4E174499772Q39411290-F7CD155E-DEAA-41EC-85D5-CF1063F4C55FQ39913720-A0A70A37-AF96-470B-B106-19DD325309F0Q40830221-98AC40A8-6CB6-439A-BB48-985F4AD192E6Q41458926-8F863C81-11EC-46ED-8389-556F432E4BBDQ41997193-93CB4DAB-473C-4310-9749-847CFECDCF34Q42978757-68668DCA-ACAC-4A93-B7F6-616E61A4C816Q43023970-EE4E5790-585F-4AFC-80B6-32A95ACCAA64Q43647837-1BE73714-27B1-4EE8-AC45-C10D35C45526Q45207785-5E22A0BA-861B-4972-9FFF-6F1AF3741E5DQ45269442-065E511F-1113-4FDF-A08E-DE297648F1F0Q45304449-C63B9934-A363-41EE-BB32-C110F06913B7Q46874381-71414D29-F6FE-42FE-A13C-0E258DB8743DQ46945937-883E18B4-C6C0-4C3B-B1B1-E9923BD5A763Q48051936-06994555-77F3-45AA-BC1B-5D318636433AQ50483669-7CB9F556-A437-4A75-ABD4-B5C310281F3CQ50910331-5351AC10-C06B-444E-9B4B-309B057A8007Q52077723-21C0FE43-BC20-4008-91B2-86F7F5427ED3Q52078727-613EF9CD-7A1E-4202-9657-D4F1285E5A84Q53817763-E4302F57-6BFE-4070-816F-EA94542CF485Q61622059-BFE00792-FBBB-4A51-A084-65BB17762815Q63214349-3DDB7666-27D9-45E9-A1D7-0B2B90EAAB82Q63214351-1710B4B5-2936-48DD-8722-B0B8B18A4CBEQ63214353-FFDA53E2-7581-4A15-868D-77C33B746E13Q79393444-ED7FB5A3-9723-4E24-9A63-3FD6176F0B43Q80479374-C2A1CFAE-82AC-4284-BADE-F9EAA393FE07
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Bjørn Olav Brandsdal
@ast
Bjørn Olav Brandsdal
@en
Bjørn Olav Brandsdal
@es
Bjørn Olav Brandsdal
@sl
type
label
Bjørn Olav Brandsdal
@ast
Bjørn Olav Brandsdal
@en
Bjørn Olav Brandsdal
@es
Bjørn Olav Brandsdal
@sl
prefLabel
Bjørn Olav Brandsdal
@ast
Bjørn Olav Brandsdal
@en
Bjørn Olav Brandsdal
@es
Bjørn Olav Brandsdal
@sl
P106
P1153
6603399441
P21
P31
P496
0000-0002-4681-8081