Interaction Details


Details of experiments between Q9P202 and Q14160
Note that the results of all experiments are listed, regardless of the modification states of the fragments.


Experiment series 1

Protein A

Protein: DFNB31
Fragment: 898-907
Site: PBM
Sequence: FLVTEFNVML
Construct: biotin-ado-ado-FLVTEFNVML

Protein B

Protein: SCRIB
Fragment: 999-1093
Site: PDZ_3
Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: 0.16
Normalized holdup BI: 0.19
Immobilized partner concentration (10-6M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
Measured pKd: 4.12
PUBMED ID: 36115835
Experimental Details

Crude peptide synthesis product. The peptide concentration in the affinity conversion step may differ from reality causing a systematic error in reported affinities.

Experiment series 2

Protein A

Protein: DFNB31
Fragment: 898-907
Site: PBM
Sequence: FLVTEFNVML
Construct: biotin-ado-ado-FLVTEFNVML

Protein B

Protein: SCRIB
Fragment: 718-814
Site: PDZ_1
Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: 0.11
Normalized holdup BI: 0.11
Immobilized partner concentration (10-6M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
Measured pKd: 3.86
PUBMED ID: 36115835
Experimental Details

Crude peptide synthesis product. The peptide concentration in the affinity conversion step may differ from reality causing a systematic error in reported affinities.

Experiment series 3

Protein A

Protein: DFNB31
Fragment: 565-578
Site: Internal_PBM
Construct: Biotin-GSGSGS-VSVDDVRSTSQGLSSY-CONH2

Protein B

Protein: SCRIB
Fragment: 718-814
Site: PDZ_1
Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: -0.02
Normalized holdup BI: -0.02
Immobilized partner concentration (10-6M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
PUBMED ID: 36115835

Experiment series 4

Protein A

Protein: DFNB31
Fragment: 565-578
Site: Internal_PBM
Construct: Biotin-GSGSGS-VSVDDVRSTSQGLSSY-CONH2

Protein B

Protein: SCRIB
Fragment: 858-949
Site: PDZ_2
Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: 0
Normalized holdup BI: 0
Immobilized partner concentration (10-6M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
PUBMED ID: 36115835

Experiment series 5

Protein A

Protein: DFNB31
Fragment: 565-578
Site: Internal_PBM
Construct: Biotin-GSGSGS-VSVDDVRSTSQGLSSY-CONH2

Protein B

Protein: SCRIB
Fragment: 999-1093
Site: PDZ_3
Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: -0.03
Normalized holdup BI: -0.03
Immobilized partner concentration (10-6M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
PUBMED ID: 36115835

Experiment series 6

Protein A

Protein: DFNB31
Fragment: 898-907
Site: PBM
Sequence: FLVTEFNVML
Construct: biotin-ado-ado-FLVTEFNVML

Protein B

Protein: SCRIB
Fragment: 858-949
Site: PDZ_2
Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: 0.01
Normalized holdup BI: 0.01
Immobilized partner concentration (10-6M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
PUBMED ID: 36115835
Experimental Details

Crude peptide synthesis product. The peptide concentration in the affinity conversion step may differ from reality causing a systematic error in reported affinities.