Information for Peptide: DQIPELENNEK from MYC_HUMAN

1. Biological Peptide

1.1 Native Sequence

    R.DQIPELENNEK.A

1.2 Peptide Properties

Start	Stop	MW	m/z for 2+	m/z for 3+	pI
379	389	1327.63	664.82	443.55	4.0

1.3 Fragment Ion Table

AA	b Ion Series	b Ion Mass	y Ion Series	y Ion Mass
D	b		y
Q	b		y
I	b		y
P	b		y
E	b		y
L	b		y
E	b		y
N	b		y
N	b		y
E	b		y
K	b		y

2. Synthetic Peptide

2.1 Synthetic (Internal Standard) Peptide Sequence

DQIPDLENNEK (Modification: E5 to D )

2.2 Peptide Properties

MW	m/z for 2+	m/z for 3+	pI
1313.61	657.81	438.88	3.92

2.3 Fragment Ion Table

AA	b Ion Series	b Ion Mass	y Ion Series	y Ion Mass
D	b		y
Q	b		y
I	b		y
P	b		y
D	b		y
L	b		y
E	b		y
N	b		y
N	b		y
E	b		y
K	b		y

2.4 Peptide Synthesis Report

Click to view/download synthesis report for DQIPELENNEK

2.5 QqQ MS/MS

Transition Table:

Transition	m/z of Transition	Collision Energy
y10	1199.59	43.0
y9	1071.53	20.0
y8	958.45	18.0
y7	861.4	26.0
y6	746.37	25.0
y5	633.28	18.0
y4	504.24	22.0
y3	390.2	37.0

2.6 Calibration Curve of Standard

Description: Dilution Curve performed on Internal standard peptide from 50 fmol to 0.1 fmol. Peptide sensitivity was detectable to 0.5 fmol.

 

Experiment Description: Cells from colon caner line HCT 116 were lysed in 8M urea/ 100mM ammonium bicarbonate buffer on ice. The equivalent of 100,000 cells were loaded onto a SDS gel. The protein of interest was excised and ingel digestion with trypsin was performed after reduction and alkylation with TCEP and IAA. 1/4 of the resulting digest was then analyzed on a Thermo Scientific TSQ mass spectrometer. Sample was analyzed concurrently with internal standard

2.7 LC-MRM Analysis of Biological and Standard Peptides Illustrates Elution Times

2.8 Pseudo MS/MS Comparison of Transition Patterns for Biological/Standard Peptides