Details of experiments between  Q15418  and Q02410  Note that the results of all experiments are listed, regardless of the modification states of the fragments.
   Experiment series 1 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPSTTL 
Protein B Protein: APBA1  Fragment: 655-741  Site: PDZ_1  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  0.01 
Normalized holdup BI:  0.01 
Immobilized partner concentration (10-6 M):  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. 
    Experiment series 2 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPSTTL 
Protein B Protein: APBA1  Fragment: 655-741  Site: PDZ_1  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  -0.03 
Holdup BI standard deviation:  0.05 
Immobilized partner concentration (10-6 M):  31 
Experiment method:  CALIP_holdup 
Details of affinity fitting:  BSA and lysozyme internal standards + bacterial cell lysate + normal layout 
Number of measurements:  4 
The affinity was below the detection threshold of the assay. 
   Experiment series 3 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPSTTL 
Protein B Protein: APBA1  Fragment: 743-822  Site: PDZ_2  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  0.03 
Normalized holdup BI:  0.04 
Immobilized partner concentration (10-6 M):  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. 
   Experiment series 4 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPSTTL 
Protein B Protein: APBA1  Fragment: 743-822  Site: PDZ_2  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  0.04 
Holdup BI standard deviation:  0.05 
Immobilized partner concentration (10-6 M):  31 
Experiment method:  CALIP_holdup 
Details of affinity fitting:  BSA and lysozyme internal standards + bacterial cell lysate + normal layout 
Number of measurements:  4 
The affinity was below the detection threshold of the assay. 
   Experiment series 5 Protein A Protein: RPS6KA1  Fragment: 726-735  Site: PBM  Sequence: RVRKLPSTTL  Construct: Biotin-ado-ado-RVRKLPSTTL 
Protein B Protein: APBA1  Fragment: 655-741  Site: PDZ_1  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  -0 
Normalized holdup BI:  -0 
Immobilized partner concentration (10-6 M):  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. 
Experimental Details Crude peptide synthesis product. The peptide concentration in the affinity conversion step may differ from reality. Not reported internal standards of holdup layout #6
   Experiment series 6 Protein A Protein: RPS6KA1  Fragment: 726-735  Site: PBM  Sequence: RVRKLPSTTL  Construct: Biotin-ado-ado-RVRKLPSTTL 
Protein B Protein: APBA1  Fragment: 743-822  Site: PDZ_2  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  0.01 
Normalized holdup BI:  0.01 
Immobilized partner concentration (10-6 M):  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. 
Experimental Details Crude peptide synthesis product. The peptide concentration in the affinity conversion step may differ from reality. Not reported internal standards of holdup layout #6
   Experiment series 7 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Modification: (SEP)732  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPpSTTL 
Protein B Protein: APBA1  Fragment: 655-741  Site: PDZ_1  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  0.06 
Normalized holdup BI:  0.06 
Immobilized partner concentration (10-6 M):  15 
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 pK d : 3.61 
Experimental Details not reported internal standards of holdup layout #5
   Experiment series 8 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Modification: (SEP)732  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPpSTTL 
Protein B Protein: APBA1  Fragment: 655-741  Site: PDZ_1  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  -0.03 
Normalized holdup BI:  -0.03 
Immobilized partner concentration (10-6 M):  15 
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. 
   Experiment series 9 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Modification: (SEP)732  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPpSTTL 
Protein B Protein: APBA1  Fragment: 655-741  Site: PDZ_1  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  0.04 
Holdup BI standard deviation:  0.05 
Immobilized partner concentration (10-6 M):  40 
Experiment method:  CALIP_holdup 
Details of affinity fitting:  BSA and lysozyme internal standards + bacterial cell lysate + normal layout 
Number of measurements:  3 
The affinity was below the detection threshold of the assay. 
   Experiment series 10 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Modification: (SEP)732  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPpSTTL 
Protein B Protein: APBA1  Fragment: 743-822  Site: PDZ_2  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  -0.03 
Normalized holdup BI:  -0.04 
Immobilized partner concentration (10-6 M):  15 
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. 
   Experiment series 11 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Modification: (SEP)732  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPpSTTL 
Protein B Protein: APBA1  Fragment: 743-822  Site: PDZ_2  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  0.02 
Normalized holdup BI:  0.02 
Immobilized partner concentration (10-6 M):  15 
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. 
Experimental Details not reported internal standards of holdup layout #5
   Experiment series 12 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Modification: (SEP)732  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPpSTTL 
Protein B Protein: APBA1  Fragment: 743-822  Site: PDZ_2  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  -0.1 
Holdup BI standard deviation:  0.05 
Immobilized partner concentration (10-6 M):  40 
Experiment method:  CALIP_holdup 
Details of affinity fitting:  BSA and lysozyme internal standards + bacterial cell lysate + normal layout 
Number of measurements:  2 
The affinity was below the detection threshold of the assay. 
   Experiment series 13 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Modification: (TPO)733  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPSpTTL 
Protein B Protein: APBA1  Fragment: 655-741  Site: PDZ_1  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  -0.02 
Normalized holdup BI:  -0.02 
Immobilized partner concentration (10-6 M):  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. 
   Experiment series 14 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Modification: (TPO)733  Sequence: RVRKLPSTTL  Construct: biotin-ttds-RRVRKLPSpTTL 
Protein B Protein: APBA1  Fragment: 743-822  Site: PDZ_2  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  0.02 
Normalized holdup BI:  0.02 
Immobilized partner concentration (10-6 M):  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. 
   Experiment series 15 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Modification: (TPO)734  Sequence: RVRKLPSTTL  Construct: Biotin-ttds-RRVRKLPSTpTL  
Protein B Protein: APBA1  Fragment: 655-741  Site: PDZ_1  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  0.08 
Normalized holdup BI:  0.08 
Immobilized partner concentration (10-6 M):  25 
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 pK d : 3.56 
   Experiment series 16 Protein A Protein: RPS6KA1  Fragment: 725-735  Site: PBM  Modification: (TPO)734  Sequence: RVRKLPSTTL  Construct: Biotin-ttds-RRVRKLPSTpTL  
Protein B Protein: APBA1  Fragment: 743-822  Site: PDZ_2  Construct: his6-MBP-TEVsite-PDZ 
Average holdup BI:  0.03 
Normalized holdup BI:  0.04 
Immobilized partner concentration (10-6 M):  25 
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. 
    
 
Please cite ProfAff! (Gogl, G. et al., Nature Communications 2022)  
© The ProfAff database is developped by the research team of Gergo Gogl .