1
在地址栏填入http://web.expasy.org/protparam/，跳转到如下： ProtParam tool
ProtParam (References / Documentation) is a tool which allows the computation of various physical and chemical parameters for a given protein stored in Swiss-Prot or TrEMBL or for a user entered
sequence. The computed parameters include the molecular weight, theoretical pI, amino acid composition, atomic composition, extinction coefficient, estimated half-life, instability index, aliphatic index and grand average of hydropathicity (GRAVY) (Disclaimer).
Please note that you may only fill out one of the following fields at a time.
Enter a Swiss-Prot/TrEMBL accession number (AC) (for example P05130) or a sequence identifier (ID) (for example KPC1_DROME):
Or you can paste your own sequence in the box below:
RESET Compute parameters 在上方小框内填入p05130，点击computer parameters，跳转到如下： ProtParam
Selection of endpoints on the sequence KPC1_DROME (P05130)
Protein kinase C, brain isozyme (EC 2.7.11.13) (PKC) (dPKC53E(BR))
Drosophila melanogaster (Fruit fly).
Please select one of the following features by clicking on a pair of endpoints, and the computation will be carried out for the corresponding sequence fragment. By default, the complete sequence is used.
Note: Only the features corresponding to subsequences of at least 5 residues are highlighted.
FT CHAIN 1-679 Protein kinase C, brain isozyme.
FT DOMAIN 191-278 C2.
FT DOMAIN 350-608 Protein kinase.
FT DOMAIN 609-679 AGC-kinase C-terminal. FT ZN_FING 45-104 Phorbol-ester/DAG-type 1. FT ZN_FING 119-169 Phorbol-ester/DAG-type 2. FT NP_BIND 356-364 ATP (By similarity).
Or, if you wish to select a different sequence fragment (at least 5 amino acids long), you can enter the desired endpoints on the
sequence here (by default, the computation will be carried out for the complete sequence). N-terminal: C-terminal: The sequence KPC1_DROME consists of 679 amino acids.
RESET SUBMIT
默认状态下打开点击submit，为完整序列计算，显示如下： ProtParam
KPC1_DROME (P05130)
Protein kinase C, brain isozyme (EC 2.7.11.13) (PKC) (dPKC53E(BR))
Drosophila melanogaster (Fruit fly).
The computation has been carried out on the complete sequence (679 amino acids).
Warning: All computation results shown below do not take into account
any annotated post-translational modification. References and documentation are available.
Please note the modified algorithm for extinction coefficient.
Number of amino acids: 679
Molecular weight: 77694.9
Theoretical pI: 6.77
Amino acid composition: Ala (A) 28 4.1% Arg (R) 26 3.8% Asn (N) 29 4.3% Asp (D) 52 7.7% Cys (C) 23 3.4% Gln (Q) 28 4.1% Glu (E) 44 6.5% Gly (G) 48 7.1% His (H) 16 2.4% Ile (I) 35 5.2% Leu (L) 51 7.5% Lys (K) 68 10.0% Met (M) 18 2.7% Phe (F) 42 6.2% Pro (P) 34 5.0% Ser (S) 34 5.0% Thr (T) 31 4.6% Trp (W) 8 1.2% Tyr (Y) 24 3.5% Val (V) 40 5.9% Pyl (O) 0 0.0% Sec (U) 0 0.0%
(B) 0 0.0%
CSV format
(Z) 0 0.0% (X) 0 0.0%
Total number of negatively charged residues (Asp + Glu): 96 Total number of positively charged residues (Arg + Lys): 94
Atomic composition:
Carbon C 3477 Hydrogen H 5374 Nitrogen N 922 Oxygen O 1018 Sulfur S 41
Formula: C3477H5374N922O1018S41
Total number of atoms: 10832
Extinction coefficients:
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
Ext. coefficient 81135
Abs 0.1% (=1 g/l) 1.044, assuming all pairs of Cys residues form cystines
Ext. coefficient 79760
Abs 0.1% (=1 g/l) 1.027, assuming all Cys residues are reduced
Estimated half-life:
The N-terminal of the sequence considered is M (Met).
The estimated half-life is: 30 hours (mammalian reticulocytes, in vitro).
>20 hours (yeast, in vivo).
>10 hours (Escherichia coli, in vivo).
Instability index:
The instability index (II) is computed to be 37.98
This classifies the protein as stable.
Aliphatic index: 70.60
Grand average of hydropathicity (GRAVY): -0.517
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在地址栏填入http://web.expasy.org/protscale/，跳转到如下： ProtScale
ProtScale [Reference / Documentation] allows you to compute and represent the profile produced by any amino acid scale on a selected protein.
An amino acid scale is defined by a numerical value assigned to each type of amino acid. The most frequently used scales are the hydrophobicity or hydrophilicity scales and the secondary structure conformational parameters scales, but many other scales exist which are based on different chemical and physical properties of the amino acids. This program provides 57 predefined scales entered from the literature.
Enter a UniProtKB/Swiss-Prot or UniProtKB/TrEMBL accession number (AC) (e.g. P05130) or a sequence identifier (ID) (e.g. KPC1_DROME):
Or you can paste your own sequence in the box below: Please choose an amino acid scale from the following list. To display information about a scale (author, reference, amino acid scale values) you can click on its name.
Molecular weight Bulkiness Polarity / Grantham
Number of codon(s) Polarity / Zimmerman Refractivity