T-Pro

Thermodynamics of Proteins and Mutants



Displayed data


The data collected in T-Pro database are organized reporting the following fields for each record:

Entry: 
Record identifier of the database.
Protein: 
Common name of the protein.
Source: 
Source of the protein.
Length: 
Total number of Amino Acid residues in the protein.
Mol. Weight: 
Molecular weight calculated considering the amino acid sequence with NC terminals and mutations.
UniProt: 
Protein identifier in UniProt database. It is also reported as SWISSPROT_ID.
EC Number: 
Enzyme Commission number.
PDB: 
Protein Data Bank code of the wild-type protein. It is also reported as PDB_wild.
PDB mutant: 
Protein Data Bank code of the mutant protein.
Chain: 
Protein chain in the PDB file. It is also reported ad MUTATED_CHAIN.
Mutation: 
Mutation with format XPOSY (X/Y: wild-type/mutant residue, POS: PDB of Sequence position).
No. Molecule: 
Number of Molecules (e.g. 1 = Monomer, 2 = Dimer, etc.).
Sec. Structure: 
Protein secondary structure of the wild-type residue (Helix,Sheet,Turn,Coil).
ASA: 
Relative solvent accessibility of the wild-type residue.
T: 
Temperature (°C).
pH: 
The pH value of the experiment.
Buffer: 
Name of the buffer used in the experiment. It is also indicated with BUFFER_NAME.
Buffer Conc.: 
Concentration of the buffer in the experiment. It is also indicated with BUFFER_CONC and [BUFFER].
Ion: 
Name of the Ions added during the experiment. It is also indicated with ION_NAME.
Additives: 
Details about the additives (e.g. glycerol).
Protein Conc.: 
Concentration of the protein when the experiment has been performed.
Measure: 
Experiment for determining the thermodynamic measures.
Method: 
Denaturation method.
ΔGH2O: 
Unfolding free energy at zero denaturant concentration (kcal/mol).
ΔΔGH2O: 
ΔGH2O(mutant) - ΔGH2O(wild-type).
ΔGu: 
Unfolding free energy in presence of denaturant(kcal/mol).
ΔΔGu: 
ΔGu(mutant) - ΔGu(wild-type). or obtained by Schellman equation.
Tm: 
Midpoint temperature for thermal denaturation methods [°C].
ΔTm: 
Tm(mutant) - Tm(wild) [°C].
ΔHvH: 
van't Hoff enthalpy change of denaturation (enthalpy obtained from the temperature dependence of the denaturation equilibrium constant).
ΔHcal: 
Calorimetric enthalpy change of denaturation (enthalpy measured by calorimetry).
m: 
Slope of ΔG on denaturant concentration (ΔG vs urea/GdnHCl; ΔG=ΔG(H2O)-m[Denaturant]) [kcal/mol/M].
Cm: 
Concentration of denaturant at which 50% of the protein is unfolded [M].
ΔCp: 
Heat capacity change of denaturation [kcal/mol/K].
State: 
Number of transition states.
Reversibility: 
Reversibility of denaturation process.
Activity: 
Specific activity of each mutant (in percentage).
Activity Km: 
Michaelis-Menten constant (substrate concentration at half maximal rate, Vmax/2) [mM].
Activity Kcat: 
Michaelis-Menten constant (rate constant) [1/s].
Activity Kd: 
Dissociation constant [mM].
Remarks: 
Comments on the reported data.
Author: 
Name of the authors.
Reference: 
Journal and voluome of the publication.
PMID: 
PubMed ID of the publication.
Related Entries: 
Identifier of the data extracted from the same publication.
Keywords: 
List of keywords used for the specific protein/article.
Review date: 
Date of the last modification of the data.



Parsable Output


All the data returned by the query search can be locally downloaded from the server. The file is a tab separated file that reports all the information described above.