| scholarly article | Q13442814 |
| P2093 | author name string | Plückthun A | |
| Jäger M | |||
| P2860 | cites work | Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A | Q27728519 |
| Mechanisms and uses of hydrogen exchange | Q30424220 | ||
| Detection of transient protein folding populations by mass spectrometry | Q34344353 | ||
| Engineered turns of a recombinant antibody improve its in vivo folding | Q36706337 | ||
| Folding and association of proteins | Q39696106 | ||
| Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant | Q41122945 | ||
| X-ray crystallography of antibodies. | Q41202692 | ||
| Solvent-induced conformational changes of polypeptides probed by electrospray-ionization mass spectrometry | Q41992607 | ||
| Beta-turn propensities as paradigms for the analysis of structural motifs to engineer protein stability | Q42845452 | ||
| Sequence statistics reliably predict stabilizing mutations in a protein domain | Q56903911 | ||
| Parallel pathways in the folding of a short-term denatured scFv fragment of an antibody | Q57696107 | ||
| Different Equilibrium Stability Behavior of ScFv Fragments: Identification, Classification, and Improvement by Protein Engineering† | Q57840032 | ||
| Domain interactions in antibody Fv and scFv fragments: effects on unfolding kinetics and equilibria | Q57840036 | ||
| Folding and assembly of an antibody Fv fragment, a heterodimer stabilized by antigen 1 1Edited by P. E. Wright | Q57840038 | ||
| Removal of the conserved disulfide bridges from the scfv fragment of an antibody: effects on folding kinetics and aggregation | Q57840042 | ||
| Comparison of the amide proton exchange behavior of the rapidly formed folding intermediate and the native state of an antibody scFv fragment | Q57840088 | ||
| The rate-limiting steps for the folding of an antibody scFv fragment | Q57840105 | ||
| Folding Nuclei of the scFv Fragment of an Antibody† | Q57840110 | ||
| Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy | Q57840153 | ||
| Evidence for a molten globule state as a general intermediate in protein folding | Q68738248 | ||
| Amide proton exchange as a probe of protein folding pathways | Q69647537 | ||
| P433 | issue | 3 | |
| P921 | main subject | refolding | Q3935998 |
| P304 | page(s) | 552-563 | |
| P577 | publication date | 2000-03-01 | |
| P1433 | published in | Protein Science | Q7251445 |
| P1476 | title | Direct evidence by H/D exchange and ESI-MS for transient unproductive domain interaction in the refolding of an antibody scFv fragment | |
| P478 | volume | 9 |
| Q44009129 | A kinetic trap is an intrinsic feature in the folding pathway of single-chain Fv fragments |
| Q44819923 | Amide hydrogen exchange/mass spectrometry applied to cooperative protein folding: equilibrium unfolding of Staphylococcus aureus aldolase |
| Q42101130 | Asymmetric effect of domain interactions on the kinetics of folding in yeast phosphoglycerate kinase. |
| Q74140438 | Current awareness |
| Q44385056 | Identification of the degradation product of ezlopitant, a non-peptidic substance P antagonist receptor, by hydrogen deuterium exchange, electrospray ionization tandem mass spectrometry (ESI/MS/MS) and nuclear magnetic resonance (NMR) spectroscopy |
| Q74134127 | Mass spectral characterization of tetracyclines by electrospray ionization, H/D exchange, and multiple stage mass spectrometry |
| Q78067723 | Partially structured state of the functional VH domain of the mouse anti-ferritin antibody F11 |
| Q35136756 | Protein-folding kinetics and mechanisms studied by pulse-labeling and mass spectrometry |
| Q34811742 | Studies of biomolecular conformations and conformational dynamics by mass spectrometry |
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