about
pH-dependent structural changes at the Heme-Copper binuclear center of cytochrome c oxidaseTechnical Decision Making With Higher Order Structure Data: Perspectives on Higher Order Structure Characterization From the Biopharmaceutical Industry.Aggregation and pH-temperature phase behavior for aggregates of an IgG2 antibody.Active site structure of the aa3 quinol oxidase of Acidianus ambivalens.Modulation of the active site conformation by site-directed mutagenesis in cytochrome c oxidase from Paracoccus denitrificans.Conformational change due to reduction of cytochrome-c oxidase in lauryl maltoside: picosecond time-resolved tryptophan fluorescence studies on the native and heat modified enzyme.Protein particulate detection issues in biotherapeutics development--current status.Comparative study of therapeutic antibody candidates derived from mini-pool and clonal cell lines.A Biopharmaceutical Industry Perspective on the Control of Visible Particles in Biotechnology-Derived Injectable Drug Products.Characterization of Aggregation Propensity of a Human Fc-Fusion Protein Therapeutic by Hydrogen/Deuterium Exchange Mass Spectrometry.Heterogeneous glycoform separation by process chromatography: I: Monomer purification and characterization.Mechanism of response of potential-sensitive dyes studied by time-resolved fluorescence.Ligand binding in the ferric and ferrous states of Paramecium hemoglobin.Potential aggregation prone regions in biotherapeutics: A survey of commercial monoclonal antibodies.Ca(2+)-binding site in Rhodobacter sphaeroides cytochrome C oxidase.Investigation of Color in a Fusion Protein Using Advanced Analytical Techniques: Delineating Contributions from Oxidation Products and Process Related Impurities.Mapping the Binding Interface in a Noncovalent Size Variant of a Monoclonal Antibody Using Native Mass Spectrometry, Hydrogen-Deuterium Exchange Mass Spectrometry, and Computational Analysis.Interference from Proteins and Surfactants on Particle Size Distributions Measured by Nanoparticle Tracking Analysis (NTA).Distal heme pocket conformers of carbonmonoxy derivatives of Ascaris hemoglobin: evidence of conformational trapping in porous sol-gel matrices.Codon-Directed Determination of the Biological Causes of Sequence Variants in Therapeutic Proteins.Identification and quantification of signal peptide variants in an IgG1 monoclonal antibody produced in mammalian cell lines.Submicron Protein Particle Characterization using Resistive Pulse Sensing and Conventional Light Scattering Based Approaches.Isomerization and Oxidation in the Complementarity-Determining Regions of a Monoclonal Antibody: A Study of the Modification-Structure-Function Correlations by Hydrogen-Deuterium Exchange Mass Spectrometry.Effect of Adriamycin on the boundary lipid structure of cytochrome c oxidase: pico-second time-resolved fluorescence depolarization studies.Challenges and new frontiers in analytical characterization of antibody-drug conjugates.The post-translational modification in cytochrome c oxidase is required to establish a functional environment of the catalytic site.Structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC6803 reveal a unique distal heme pocketIdentification of the Ligands to the Ferric Heme ofChlamydomonasChloroplast Hemoglobin: Evidence for Ligation of Tyrosine-63 (B10) to the Heme†Folding of cytochrome c initiated by submillisecond mixingTime-resolved study of tryptophan fluorescence in vesicle reconstituted cytochrome oxidase. Effect of redox transitionOrigin of the anomalous Fe-CO stretching mode in the CO complex of Ascaris hemoglobinMutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme aRedox-linked conformational changes in bovine heart cytochrome c oxidase: picosecond time-resolved fluorescence studies of cyanide complexThe apolar distal histidine mutant (His69-->Val) of the homodimeric Scapharca hemoglobin is in an R-like conformationNMR studies on interaction of lauryl maltoside with cytochrome c oxidase: a model for surfactant interaction with the membrane proteinHydroxide rather than histidine is coordinated to the heme in five-coordinate ferric Scapharca inaequivalvis hemoglobinThe heme environment in barley hemoglobinImpact of denaturation with urea on recombinant apolipoprotein A-IMilano ion-exchange adsorption: equilibrium uptake behavior and protein mass transfer kineticsInvestigation of PEG crystallization in frozen and freeze-dried PEGylated recombinant human growth hormone-sucrose systems: implications on storage stabilityCharacterization of therapeutic antibody fragmentation using automated capillary western blotting as an orthogonal analytical technique
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Q28363670-A1672014-A0C6-4F09-B10E-7C20F912DF27Q30394137-4152754C-37CD-4E91-B5FE-972D08EBE88CQ34127986-6FDE0F80-15CF-4673-B818-9ABE90A9ED30Q35752166-217E42B3-519A-44A7-9A19-C5AE936B8C1AQ36162910-7C716541-1EF7-4D3F-B1EA-92983DD1698DQ36711155-82FB2EB4-D172-4231-8F38-CCC10A0BA3E7Q38008257-6FA84E8D-0814-4426-9BD4-482C79B41B20Q38557922-F522FDD2-EE4E-431B-945A-7C7D1AC86898Q38811592-A9F9BB6F-BDF2-49E5-90CA-B3BCC9483182Q39488460-CE70A061-FD5F-48EC-9D9B-087F68104DFCQ40861780-71CBC12E-1E16-4E84-A57E-E94138B5B76CQ42184762-1094179E-D0B4-4E75-8CC3-74F289CCBB89Q42637878-53B6A606-714E-4AE9-8202-3C6CD237EE1FQ43070206-984EE771-A44D-44FA-B43B-E57F7C538480Q44053258-E14A2594-F237-4232-BC78-4BC2DAE51B2EQ46624990-027AD2FA-9930-434F-8F67-8473DC08C63EQ47204822-00672290-38D6-44E7-B7A9-2D413243E3C5Q47238029-151D1582-7105-4C8D-8569-8625D8486B39Q47305676-1B469F1D-9D55-4D50-9AC9-9B95DADC05DCQ47584275-01A7DAC9-5C87-48DA-BCCB-BCE039A0B373Q47594835-042CC4BB-AB25-4679-AF48-96FE5AA2D3ACQ50052234-8A3AF43D-CA67-49E6-B54E-9C95EC066232Q51739313-EAA4F91D-4F95-45F2-AC3C-172FCA41B9BDQ52073405-0462A163-A1A4-404E-9ABC-1F1B54997CA7Q52401505-4B9460A3-D876-4063-AAB0-083546AC5A7EQ52532194-239FF8C7-91D9-495C-A1FE-51FCD943052AQ62026439-3C68C5AD-1DCF-4F25-AE4C-D6A0434BCF1DQ62026442-B13FE12F-EA41-4C27-91AA-F39A043E91E4Q71958826-0FC3153E-3C82-49B2-A579-1751573D4548Q72659585-BDF95A75-DD8A-4052-B5FB-0E7B96956B03Q73395020-E47C6C08-0030-472F-9898-99D139B90DEAQ73543772-CB892D4A-22D1-4077-B539-1745787D3F96Q74221824-F8FCA77F-CA09-49BE-8D3C-FEB0B2DE7793Q74457502-73143B11-E234-4A4D-81B4-60B5056C5F28Q74472048-210C8B8D-488E-41F1-A45A-6AE7033B60C7Q77896919-A4B55050-6ED3-46C5-877E-A6107B13ED6CQ77953997-F092EAD3-DB2B-4655-A0F7-688DC1544A8DQ79395003-1F0674A4-922C-4740-AA6D-80EA9AB34936Q83859483-10EEA12F-4F09-426A-BFCF-922A87CB0E0FQ91604014-0A772D89-0511-4922-8621-CEFD58DE42AF
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Tapan K Das
@nl
Tapan K Das
@sl
Tapan K. Das
@en
Tapan K. Das
@es
type
label
Tapan K Das
@nl
Tapan K Das
@sl
Tapan K. Das
@en
Tapan K. Das
@es
prefLabel
Tapan K Das
@nl
Tapan K Das
@sl
Tapan K. Das
@en
Tapan K. Das
@es
P106
P1153
55664463600
P31
P496
0000-0002-3641-3988