A calorimetric study of thermally induced conformational transitions of ribonuclease A and certain of its derivatives.

Abstract

Study holds ProTherm entries: 7334, 7335, 7336, 7337, 7338, 7339, 7340, 7341, 7342, 7343, 7344, 7345, 7346, 7347, 7348, 7349, 7350, 7351, 7352, 7353 Extra Details: conformational transition; cooperativity; two-state process;,calorimatric measurement

Submission Details

ID: DLsq5XWV4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:33 p.m.

Version: 1

Publication Details
Tsong TY;Hearn RP;Wrathall DP;Sturtevant JM,Biochemistry (1970) A calorimetric study of thermally induced conformational transitions of ribonuclease A and certain of its derivatives. PMID:5465355
Additional Information

Study Summary

Number of data points 60
Proteins Ribonuclease pancreatic ; Ribonuclease pancreatic
Unique complexes 1
Assays/Quantities/Protocols Experimental Assay: dHcal ionic:NaCl: 0.2 N, pH:1.05, buffers:HCl: - ; Experimental Assay: Tm ionic:NaCl: 0.2 N, pH:1.05, buffers:HCl: - ; Experimental Assay: dHcal ionic:HCl: , pH:0.36, buffers:HCl: - ; Experimental Assay: Tm ionic:HCl: , pH:0.36, buffers:HCl: - ; Experimental Assay: dCp ionic:NaCl: 0.2 N, buffers:None: -, pH:7.8 ; Experimental Assay: dHcal ionic:NaCl: 0.2 N, buffers:None: -, pH:7.8 ; Experimental Assay: Tm ionic:NaCl: 0.2 N, buffers:None: -, pH:7.8 ; Experimental Assay: dHvH ionic:NaCl: 0.2 N, buffers:None: -, pH:7.8 ; Experimental Assay: dCp ionic:NaCl: 0.2 N, buffers:None: -, pH:7.0 ; Experimental Assay: dHcal ionic:NaCl: 0.2 N, buffers:None: -, pH:7.0 ; Experimental Assay: Tm ionic:NaCl: 0.2 N, buffers:None: -, pH:7.0 ; Experimental Assay: dHvH ionic:NaCl: 0.2 N, buffers:None: -, pH:7.0 ; Experimental Assay: dCp pH:6.23, ionic:: , buffers:acetate: 0.2 N ; Experimental Assay: dHcal pH:6.23, ionic:: , buffers:acetate: 0.2 N ; Experimental Assay: Tm pH:6.23, ionic:: , buffers:acetate: 0.2 N ; Experimental Assay: dHvH pH:6.23, ionic:: , buffers:acetate: 0.2 N ; Experimental Assay: dCp pH:5.0, ionic:: , buffers:acetate: 0.2 N ; Experimental Assay: dHcal pH:5.0, ionic:: , buffers:acetate: 0.2 N ; Experimental Assay: Tm pH:5.0, ionic:: , buffers:acetate: 0.2 N ; Experimental Assay: dHvH pH:5.0, ionic:: , buffers:acetate: 0.2 N ; Experimental Assay: dCp ionic:: , buffers:acetate: 0.2 N, pH:4.04 ; Experimental Assay: dHcal ionic:: , buffers:acetate: 0.2 N, pH:4.04 ; Experimental Assay: Tm ionic:: , buffers:acetate: 0.2 N, pH:4.04 ; Experimental Assay: dHvH ionic:: , buffers:acetate: 0.2 N, pH:4.04 ; Experimental Assay: dCp ionic:: , pH:3.28, buffers:glycine: 0.2 N ; Experimental Assay: dHcal ionic:: , buffers:glycine: 0.2 N, pH:3.28 ; Experimental Assay: Tm ionic:: , pH:3.28, buffers:glycine: 0.2 N ; Experimental Assay: dHvH ionic:: , pH:3.28, buffers:glycine: 0.2 N ; Experimental Assay: dCp pH:2.8, ionic:: , buffers:glycine: 0.2 N ; Experimental Assay: dHcal pH:2.8, ionic:: , buffers:glycine: 0.2 N ; Experimental Assay: Tm pH:2.8, ionic:: , buffers:glycine: 0.2 N ; Experimental Assay: dHvH ionic:: , pH:2.8, buffers:glycine: 0.2 N ; Experimental Assay: dCp pH:2.02, ionic:: , buffers:glycine: 0.2 N ; Experimental Assay: dHcal pH:2.02, ionic:: , buffers:glycine: 0.2 N ; Experimental Assay: Tm pH:2.02, ionic:: , buffers:glycine: 0.2 N ; Experimental Assay: dHvH pH:2.02, ionic:: , buffers:glycine: 0.2 N ; Experimental Assay: dCp ionic:NaCl: 0.1 N, pH:1.05, buffers:glycine: 0.2 N ; Experimental Assay: dHcal ionic:NaCl: 0.1 N, pH:1.05, buffers:glycine: 0.2 N ; Experimental Assay: Tm ionic:NaCl: 0.1 N, pH:1.05, buffers:glycine: 0.2 N ; Experimental Assay: dHvH ionic:NaCl: 0.1 N, pH:1.05, buffers:glycine: 0.2 N ; Experimental Assay: dCp ionic:HCl: , buffers:glycine: 0.2 N, pH:0.36 ; Experimental Assay: dHcal ionic:HCl: , buffers:glycine: 0.2 N, pH:0.36 ; Experimental Assay: Tm ionic:HCl: , buffers:glycine: 0.2 N, pH:0.36 ; Experimental Assay: dHvH ionic:HCl: , buffers:glycine: 0.2 N, pH:0.36
Libraries Mutations for sequence KETAAAKFERQHMDSSTSAASSSNYCNQMMKSRNLTKDRCKPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHFDASV

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
6QMN 2019-02-07T00:00:00+0000 2.31 Crystal structure of a Ribonuclease A-Onconase chimera
6XHD 2020-06-18T00:00:00+0000 1.51 Structure of Prolinyl-5'-O-adenosine phosphoramidate
6XHE 2020-06-18T00:00:00+0000 1.88 Structure of beta-prolinyl 5'-O-adenosine phosphoramidate
3QL2 2011-02-02T00:00:00+0000 1.49 Crystal Structure of Ribonuclease A Variant A4C/D83E/V118C
1YMW 2005-01-21T00:00:00+0000 1.5 The study of reductive unfolding pathways of RNase A (Y92G mutant)
4G90 2012-07-23T00:00:00+0000 1.9 Crystal structure of Ribonuclease A in complex with 5e
3D6P 2008-05-20T00:00:00+0000 1.6 RNase A- 5'-Deoxy-5'-N-morpholinouridine complex
3D6Q 2008-05-20T00:00:00+0000 1.6 The RNase A- 5'-Deoxy-5'-N-piperidinouridine complex
1KH8 2001-11-29T00:00:00+0000 2.0 Structure of a cis-proline (P114) to glycine variant of Ribonuclease A
4WYP 2014-11-17T00:00:00+0000 1.5 The crystal structure of the A109G mutant of RNase A in complex with 5'AMP

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
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 P61823 RNAS1_BOVIN
100.0 Ribonuclease pancreatic P61824 RNAS1_BISBI