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Computational design of protein self-assemblyA conserved structural motif mediates formation of the periplasmic rings in the type III secretion systemStructure of the basal components of a bacterial transporterComputational Design of Self-Assembling Protein Nanomaterials with Atomic Level AccuracyA De Novo Designed Coiled-Coil Peptide with a Reversible pH-Induced Oligomerization SwitchRosettaDock in CAPRI rounds 6-12Structure prediction for CASP7 targets using extensive all-atom refinement with Rosetta@homeModeling symmetric macromolecular structures in Rosetta3Computational de novo design of a self-assembling peptide with predefined structure.Alternate states of proteins revealed by detailed energy landscape mappingStreptococcal M protein: structural studies of the hypervariable region, free and bound to human C4BP.RosettaRemodel: a generalized framework for flexible backbone protein design.Interactions of the transmembrane polymeric rings of the Salmonella enterica serovar Typhimurium type III secretion systemThe role of electrostatic interactions in calmodulin-peptide complex formation.Salt enhances calmodulin-target interaction.A vast repertoire of Dscam binding specificities arises from modular interactions of variable Ig domains.Computational design of a leucine-rich repeat protein with a predefined geometryDetermination of the structures of symmetric protein oligomers from NMR chemical shifts and residual dipolar couplings.The RosettaCon 2012 Special Collection: Code Writ on Water, Documentation Writ in Stone.Prediction of the structure of symmetrical protein assemblies.Emergence of symmetry in homooligomeric biological assemblies.Simultaneous prediction of protein folding and docking at high resolution.Automated determination of fibrillar structures by simultaneous model building and fiber diffraction refinement.pK(a) values for side-chain carboxyl groups of a PGB1 variant explain salt and pH-dependent stabilityAutomated de novo phasing and model building of coiled-coil proteins.Residue-specific pKa determination of lysine and arginine side chains by indirect 15N and 13C NMR spectroscopy: application to apo calmodulin.Calbindin D28k EF-hand ligand binding and oligomerization: four high-affinity sites--three modes of action.Electrostatic Contributions to Residue-Specific Protonation Equilibria and Proton Binding Capacitance for a Small Protein†Measurement of Ca2+-Binding Constants of Proteins and Presentation of the CaLigator SoftwareA Protein-Based Encapsulation System with Calcium-Controlled Cargo Loading and DetachmentBayesian inference of protein conformational ensembles from limited structural dataExploring alternate states and oligomerization preferences of coiled-coils by de novo structure modelingModeling the Structure of Helical Assemblies with Experimental Constraints in RosettaComputational assessment of folding energy landscapes in heterodimeric coiled coils
P50
Q26748913-174D6576-F1BE-4F7F-8F2F-EBF75EACC8E7Q27655277-85B56194-807E-4A5D-881E-F5C7FE223C02Q27678103-44B34DBF-6039-4B81-A507-4991EC9A2BC6Q27679409-D404B894-396D-42F1-A715-1CAE70680E03Q27704832-F3F01182-51FE-4C60-B3D2-6EF9AEC8D50BQ28239152-004716C2-760E-4AF2-AE5C-D939F62C7936Q28250601-5DFBFE11-7B24-4466-AFAD-E424AF7BB6E9Q28478675-814FCE1F-7E6C-456C-9F5B-D6DDA7B67B37Q30369608-44F14C4D-E2B9-4E05-95AF-0193DEFF3ADFQ30396213-54814069-38F5-45E1-B13C-5D9BAEB59859Q33238480-650D8909-BB0C-4BF0-B286-8D5A8007433FQ34016448-204873BF-79B9-401A-98A9-8AD8E7BB95B9Q34100072-1775D282-9539-40FE-9E34-A5AEA5B856DFQ34187132-BFF38D68-4457-4110-B67D-2B4E82CC7442Q34481514-9CB8BCDA-F510-469C-8D8B-F43219AA8B72Q34692066-6286975B-BD0C-43CD-912E-7E1C087FBE0BQ34752273-03CA7A74-83B1-41A3-B6E3-D48FD72E9977Q34823306-0CCF524B-402C-478E-9AB3-8071DB6EC419Q35004812-C61FC788-3D95-4815-9F84-DCC766B58C17Q36140836-EF65D136-7F01-4269-B785-F95076AA9196Q36945073-688E0A49-7FCE-46EE-B6CF-D093F249BAECQ37404702-7E4C2E29-36A3-44EC-A742-8207FFCC31E8Q40953313-300D95E3-9787-44D9-B4C4-838295879A46Q41046751-3ADE7FB9-4991-4C77-AD56-ED90C63FB344Q41246116-C59651B2-66BA-43EE-ACC4-A0F77F90FD5BQ46877470-68F5D21E-1FDC-4D83-A234-E03EF5936124Q48736968-821E421B-97C4-4967-BD2B-E1FA79DE44FFQ57904181-55927C8E-50A0-44C1-B439-C68275EE372EQ57904218-F06CE04F-0AA7-45E8-9F06-5BA7F3EF5AD2Q59357581-8DB24D89-A8FD-47E4-BF0F-1207F28554DCQ60952323-C7E77B9D-FE8C-4EA3-93A2-C5AD36E3184EQ85993131-A6504C7C-9597-4117-BF01-4DE806D524C5Q88237638-E88FFBF8-CC90-4DA0-AB97-C27FF3E82DDFQ88417979-D45BA279-C164-43C2-B1B8-DB5E74D31BBC
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Ingemar André
@ast
Ingemar André
@en
Ingemar André
@es
Ingemar André
@nl
type
label
Ingemar André
@ast
Ingemar André
@en
Ingemar André
@es
Ingemar André
@nl
altLabel
André I
@en
prefLabel
Ingemar André
@ast
Ingemar André
@en
Ingemar André
@es
Ingemar André
@nl
P1053
O-4777-2014
P106
P1153
21739430000
P31
P4012
P496
0000-0002-4753-8233