Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology.

Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology.

Item
http://www.wikidata.org/entity/Q36889497
Size of the ligand complex between the N-terminal domain of the gene III coat protein and the non-infectious phage strongly influences the usefulness of in vitro selective infective phage technology.Tailoring in vitro evolution for protein affinity or stability.Selective infection of E. coli as a function of a specific molecular interaction.A mutation designed to alter crystal packing permits structural analysis of a tight-binding fluorescein-scFv complex.A bifunctional converter: fluorescein quenching scFv/fluorogen activating protein for photostability and improved signal to noise in fluorescence experiments.Antigen binding forces of individually addressed single-chain Fv antibody molecules.Unbinding forces of single antibody-antigen complexes correlate with their thermal dissociation rates.Modulating Antibody Structure and Function through Directed Mutations and Chemical Rescue.
P2860

Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology.

Item
http://www.wikidata.org/entity/Q36889497
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Affinity and folding propertie ...... ctive phage (SIP) methodology.
@en
type
label
Affinity and folding propertie ...... ctive phage (SIP) methodology.
@en
prefLabel
Affinity and folding propertie ...... ctive phage (SIP) methodology.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Affinity and folding propertie ...... ective phage (SIP) methodology
@en
P2093
P2860
P304
P31
P356
10.1016/S0014-5793(97)01143-5
P407
P433
P478
P50
P577
P698