MPTherm
Database for Membrane Protein Thermodynamics for understanding folding and stability
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Entry name
Gene name
Organism
Protein name
UniProt ID
PDB ID
Mutation type
All
Wild-type
Single
Double
Multiple
Residue mutation from
All
Ala (A)
Arg (R)
Asn (N)
Asp (D)
Cys (C)
Gln (Q)
Glu (E)
Gly (G)
His (H)
Ile (I)
Leu (L)
Lys (K)
Met (M)
Phe (F)
Pro (P)
Ser (S)
Thr (T)
Trp (W)
Tyr (Y)
Val (V)
to
All
Ala (A)
Arg (R)
Asn (N)
Asp (D)
Cys (C)
Gln (Q)
Glu (E)
Gly (G)
His (H)
Ile (I)
Leu (L)
Lys (K)
Met (M)
Phe (F)
Pro (P)
Ser (S)
Thr (T)
Trp (W)
Tyr (Y)
Val (V)
Protein type
α-helical
β-barrel
Topology
All
Cytoplasm or Inside
Membrane
Extra-cellular or Outside
Others
Denaturation
Thermal
Chemical
Measure
All
CD
DSC
Activity
Fluorescence
T
m
to
ΔT
m
to
ΔG
H
2
O
to
ΔΔG
H
2
O
to
Author
Journal
Year
to
Display Columns
Protein information
Entry
Gene name
Organism
Protein name
UniProt ID
Length
Mutation (UniProt)
PDB ID
Mutation (PDB)
Mutation type
Protein type
Topology
No of TM segments
Experimental conditions
pH
Temperature
Buffer name
Ion name
Additives
Denaturation
Measure
Thermodynamic parameters
T
m
ΔT
m
ΔG
ΔΔG
ΔG
H
2
O
ΔΔG
H
2
O
ΔH
ΔC
p
C
m
m
Reversibility
State
Remarks
Literature
PubMed/Reference
Location
Authors
Title
Year
Volume
Pages
Journal
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