A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study.


Abstract

Study holds ProTherm entries: 12342, 12343, 12344, 12345, 12346, 12347, 12348, 12349, 12350, 12351, 12352, 12353, 12354, 12355, 12356, 12357, 12358, 12359, 12360, 12361, 12362 Extra Details: Data taken from W.Pfeil (Protein stability and folding, Springer-Verlag 1998) page 384, Ref 74P1. two-state transition; intermediates; structual paramenters; hydrogen bond

Submission Details

ID: RvBFKsZy3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:43 p.m.

Version: 1

Publication Details
Privalov PL;Khechinashvili NN,J. Mol. Biol. (1974) A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. PMID:4368360
Additional Information

Study Summary

Number of data points 56
Proteins Cytochrome c ; Myoglobin ; Ribonuclease pancreatic ; Chymotrypsinogen A ; Cytochrome c ; Lysozyme C ; Myoglobin ; Lysozyme C ; Ribonuclease pancreatic ; Calnexin
Unique complexes 5
Assays/Quantities/Protocols Experimental Assay: dCp pH:10.5 ; Experimental Assay: Tm pH:10.5 ; Experimental Assay: dHvH ; Experimental Assay: dCp pH:4.83 ; Experimental Assay: dHcal pH:4.83 ; Experimental Assay: Tm pH:4.83 ; Experimental Assay: dCp pH:4.52 ; Experimental Assay: dHcal pH:4.52 ; Experimental Assay: Tm pH:4.52 ; Experimental Assay: dCp pH:3.94 ; Experimental Assay: dHcal pH:3.94 ; Experimental Assay: Tm pH:3.94 ; Experimental Assay: dCp pH:3.75 ; Experimental Assay: dHcal pH:3.75 ; Experimental Assay: Tm pH:3.75 ; Experimental Assay: dCp pH:3.4 ; Experimental Assay: dHcal pH:3.4 ; Experimental Assay: Tm pH:3.4 ; Experimental Assay: dCp pH:3.18 ; Experimental Assay: dHcal pH:3.18 ; Experimental Assay: Tm pH:3.18 ; Experimental Assay: dCp pH:3.12 ; Experimental Assay: dHcal pH:3.12 ; Experimental Assay: Tm pH:3.12 ; Experimental Assay: dCp pH:3.05 ; Experimental Assay: dHcal pH:3.05 ; Experimental Assay: Tm pH:3.05 ; Experimental Assay: dCp pH:2.92 ; Experimental Assay: dHcal pH:2.92 ; Experimental Assay: Tm pH:2.92 ; Experimental Assay: dHcal pH:2.81 ; Experimental Assay: Tm pH:2.81 ; Experimental Assay: dCp pH:3.8 ; Experimental Assay: dHcal pH:3.8 ; Experimental Assay: Tm pH:3.8 ; Experimental Assay: dCp pH:3.3 ; Experimental Assay: dHcal pH:3.3 ; Experimental Assay: Tm pH:3.3 ; Experimental Assay: dCp pH:3.15 ; Experimental Assay: dHcal pH:3.15 ; Experimental Assay: Tm pH:3.15 ; Experimental Assay: dCp pH:2.82 ; Experimental Assay: dHcal pH:2.82 ; Experimental Assay: Tm pH:2.82 ; Experimental Assay: dCp pH:2.6 ; Experimental Assay: dHcal pH:2.6 ; Experimental Assay: Tm pH:2.6 ; Experimental Assay: dCp pH:2.44 ; Experimental Assay: dHcal pH:2.44 ; Experimental Assay: Tm pH:2.44 ; Experimental Assay: dCp pH:2.21 ; Experimental Assay: dHcal pH:2.21 ; Experimental Assay: Tm pH:2.21 ; Experimental Assay: dG_H2O temp:38.0 C, pH:4.7 ; Experimental Assay: dG_H2O temp:25.0 C, pH:7.0 ; Experimental Assay: dG_H2O pH:1.0, temp:25.0 C
Libraries Mutations for sequence KETAAAKFERQHMDSSTSAASSSNYCNQMMKSRNLTKDRCKPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHFDASV ; Mutations for sequence GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKKGEREDLIAYLKKATNE ; Mutations for sequence VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG ; Mutations for sequence KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL ; Mutations for sequence SKSKPDTSAPTSPKVTYKAPVPSGEVYFADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVDEMKETKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGVYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSIVNSGNLLNDMTPPVNPSREIEDPEDQKPEDWDERPKIPDPDAVKPDDWNEDAPAKIPDEEATKPDGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPKCESAPGCGVWQRPMIDNPNYKGKWKPPMIDNPNYQGIWKPRKIPNPDFFEDLEPFKMTPFSAIGLELWSMTSDIFFDNFIVCGDRRVVDDWANDGWGLKKAADGAAEP

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
2AIU 2005-08-01T00:00:00+0000 1.6 Crystal Structure of Mouse Testicular Cytochrome C at 1.6 Angstrom
2IHL 1993-06-29T00:00:00+0000 1.4 LYSOZYME (E.C.3.2.1.17) (JAPANESE QUAIL)
1JHN 2001-06-28T00:00:00+0000 2.9 Crystal Structure of the Lumenal Domain of Calnexin
6QMN 2019-02-07T00:00:00+0000 2.31 Crystal structure of a Ribonuclease A-Onconase chimera
1KTD 2002-01-15T00:00:00+0000 2.4 CRYSTAL STRUCTURE OF CLASS II MHC MOLECULE IEK BOUND TO PIGEON CYTOCHROME C PEPTIDE
6BMG 2017-11-14T00:00:00+0000 1.88 Structure of Recombinant Dwarf Sperm Whale Myoglobin (Oxy)
1JHL 1993-05-04T00:00:00+0000 2.4 THREE-DIMENSIONAL STRUCTURE OF A HETEROCLITIC ANTIGEN-ANTIBODY CROSS-REACTION COMPLEX
1GHL 1993-05-04T00:00:00+0000 2.1 THE THREE-DIMENSIONAL STRUCTURE OF PHEASANT AND GUINEA-FOWL EGG LYSOZYMES
1FBI 1995-01-19T00:00:00+0000 3.0 CRYSTAL STRUCTURE OF A CROSS-REACTION COMPLEX BETWEEN FAB F9.13.7 AND GUINEA-FOWL LYSOZYME
1HHL 1993-05-04T00:00:00+0000 1.9 THE THREE-DIMENSIONAL STRUCTURE OF PHEASANT AND GUINEA-FOWL EGG LYSOZYMES

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
90.3 Cytochrome c P21665 CYC_VARVA
90.4 Cytochrome c P00015 CYC2_MOUSE
90.5 Cytochrome c Q640U4 CYC1_XENTR
91.4 Cytochrome c P00022 CYC_CHESE
90.5 Cytochrome c P00019 CYC_STRCA
90.5 Cytochrome c P00018 CYC_DRONO
90.5 Cytochrome c Q5RFH4 CYC_PONAB
90.5 Cytochrome c P99998 CYC_PANTR
90.5 Cytochrome c P99999 CYC_HUMAN
90.5 Cytochrome c Q6WUX8 CYC_GORGO
90.5 Cytochrome c P00017 CYC_APTPA
91.4 Cytochrome c P67882 CYC_MELGA
91.4 Cytochrome c P67881 CYC_CHICK
94.2 Cytochrome c P00020 CYC_ANAPL
91.4 Cytochrome c Q52V08 CYC_MACSY
91.4 Cytochrome c P00002 CYC_MACMU
93.2 Cytochrome c P00021 CYC_COLLI
94.2 Cytochrome c P81280 CYC_ALLMI
91.4 Cytochrome c Q52V10 CYC_SAISC
93.2 Cytochrome c B4USV4 CYC_OTOGA
95.2 Cytochrome c P00013 CYC_MINSC
94.3 Cytochrome c P00014 CYC_MACGI
96.2 Cytochrome c P00012 CYC_MIRLE
96.2 Cytochrome c P00008 CYC_RABIT
96.2 Cytochrome c Q52V09 CYC_CEPBA
97.1 Cytochrome c P00004 CYC_HORSE
97.1 Cytochrome c P00011 CYC_CANLF
97.1 Cytochrome c P62898 CYC_RAT
97.1 Cytochrome c P62897 CYC_MOUSE
98.1 Cytochrome c P68096 CYC_EQUBU
98.1 Cytochrome c P68097 CYC_EQUAS
98.1 Cytochrome c P68098 CYC_LAMGU
98.1 Cytochrome c P68100 CYC_ESCRO
98.1 Cytochrome c P68099 CYC_CAMDR
97.1 Cytochrome c P00007 CYC_HIPAM
100.0 Cytochrome c P62896 CYC_SHEEP
100.0 Cytochrome c P62895 CYC_PIG
100.0 Cytochrome c P62894 CYC_BOVIN
90.1 Myoglobin P02182 MYG_ZIPCA
90.1 Myoglobin Q0KIY0 MYG_MESST
90.1 Myoglobin P02183 MYG_MESCA
90.3 Myoglobin P02180 MYG_BALPH
90.9 Myoglobin P02179 MYG_BALAC
90.8 Myoglobin P68278 MYG_PHOPH
90.8 Myoglobin P68277 MYG_PHODA
90.8 Myoglobin P68279 MYG_TURTR
90.8 Myoglobin P68276 MYG_DELDE
90.8 Myoglobin Q0KIY7 MYG1_STEAT
91.4 Myoglobin P02173 MYG_ORCOR
92.1 Myoglobin P02174 MYG_GLOME
91.4 Myoglobin P02181 MYG_INIGE
92.2 Myoglobin P02178 MYG_MEGNO
91.4 Myoglobin Q0KIY3 MYG_PENEL
92.9 Myoglobin P02177 MYG_ESCRO
92.9 Myoglobin Q0KIY2 MYG_BALED
92.9 Myoglobin Q0KIY1 MYG_BALBO
96.8 Myoglobin P02184 MYG_KOGSI
96.8 Myoglobin Q0KIY5 MYG_KOGBR
100.0 Myoglobin P02185 MYG_PHYMC
96.0 Ribonuclease pancreatic Q29606 RNAS1_ORYLE
90.3 Ribonuclease pancreatic P00662 RNAS1_GIRCA
92.7 Ribonuclease pancreatic P00668 RNAS1_ANTAM
95.2 Ribonuclease pancreatic P00660 RNAS1_CONTA
93.5 Ribonuclease pancreatic P07848 RNAS1_EUDTH
96.0 Ribonuclease pancreatic P07847 RNAS1_AEPME
95.2 Ribonuclease pancreatic P00657 RNAS1_BUBBU
96.8 Ribonuclease pancreatic P67927 RNAS1_SHEEP
96.8 Ribonuclease pancreatic P67926 RNAS1_CAPHI
100.0 Ribonuclease pancreatic P61824 RNAS1_BISBI
100.0 Ribonuclease pancreatic P61823 RNAS1_BOVIN
100.0 Chymotrypsinogen A P00766 CTRA_BOVIN
93.0 Lysozyme C P81711 LYSC_SYRSO
92.3 Lysozyme C P49663 LYSC_PHAVE
94.6 Lysozyme C P24533 LYSC_SYRRE
93.0 Lysozyme C P24364 LYSC_LOPLE
92.2 Lysozyme C P00704 LYSC_NUMME
95.3 Lysozyme C Q7LZT2 LYSC_TRATE
95.3 Lysozyme C P22910 LYSC_CHRAM
96.1 Lysozyme C P19849 LYSC_PAVCR
96.1 Lysozyme C Q7LZI3 LYSC_TRASA
96.9 Lysozyme C Q7LZP9 LYSC_LOPIM
96.9 Lysozyme C Q7LZQ0 LYSC_CATWA
96.9 Lysozyme C P00699 LYSC_CALCC
96.9 Lysozyme C P00700 LYSC_COLVI
93.2 Lysozyme C P00702 LYSC_PHACO
95.2 Lysozyme C P00703 LYSC_MELGA
95.3 Lysozyme C P00701 LYSC_COTJA
100.0 Lysozyme C P00698 LYSC_CHICK
96.4 Calnexin P35565 CALX_RAT
97.6 Calnexin P35564 CALX_MOUSE
96.1 Calnexin P27824 CALX_HUMAN
96.4 Calnexin Q5R440 CALX_PONAB
99.8 Calnexin P24643 CALX_CANLF