Thermostability of the barnase-barstar complex.
Abstract
Scanning microcalorimetry was used to study heat denaturation of barnase in complex with its intracellular inhibitor barstar. The heat denaturation of the barnase-barstar complex is well approximately by two two-state transitions with the lower temperature transition corresponding to barstar denaturation and the higher temperature one to barnase denaturation. The temperature of barnase melting in its complex with barstar is 20 degrees C higher than that of the free enzyme. The barstar melting temperature is almost the same in the complex or alone (71 degrees C at pH 6.2 and 68 degrees C at pH 8.0). It seems possible that when barstar unfolds it can remain bound to barnase, while the latter unfolds only on dissociation of the denatured barstar. Study holds ProTherm entries: 10386, 10387 Extra Details: barnase-barstar complex; heat denaturation; scanning microcalorimetry;,isothermal microcalorimetry
Submission Details
ID: cxAM5esa
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:40 p.m.
Version: 1
Publication Details
Makarov AA;Protasevich II;Lobachov VM;Kirpichnikov MP;Yakovlev GI;Gilli RM;Briand CM;Hartley RW,FEBS Lett. (1994) Thermostability of the barnase-barstar complex. PMID:7957933Additional Information
Study Summary
| Number of data points | 4 |
| Proteins | Ribonuclease ; Ribonuclease |
| Unique complexes | 1 |
| Assays/Quantities/Protocols | Experimental Assay: dHcal ionic:NaCl: 0.05 M ; Experimental Assay: Tm ionic:NaCl: 0.05 M ; Experimental Assay: dHcal ionic:: ; Experimental Assay: Tm ionic:: |
| Libraries | Mutations for sequence AQVINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNREGKLPGKSGRTWREADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR |
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
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Data Distribution
Studies with similar sequences (approximate matches)