High-resolution differential scanning calorimetric study of myosin, functional domains, and supramolecular structures.


High-resolution differential scanning calorimetry (DSC) has been employed to study the thermal stability of myosin, its major constitutive fragments (S-1, light chains, and rod), and also reconstituted thick filaments. The thermal denaturation of soluble myosin was complex and was characterized by a multistep endothermic process for the temperature range from 41 to 60 degrees C. The shape of the endotherm was highly dependent on the pH and the ionic strength of the solution, although the delta Hcal (calorimetric enthalpy) of denaturation (1715 +/- 75 kcal/mol) was insensitive to these changes for the solvent conditions used in this study. This value also agrees, within experimental error, with the sum of the denaturation enthalpies obtained for isolated fragments (1724 +/- 79 kcal/mol). In identical conditions of ionic strength, pH, and heating rate, the computer-calculated differential endotherms of domains belonging to S-1 and light chains were superimposable with those of the isolated fragments. Their responses to changes in the solvent condition were also similar. We suggest that the observed functional independence of the major domains in myosin reflects also the independence of their structural stability. The thermal unfolding of the isolated rod was multiphasic and readily reversible (95%). It occurred between 41 and 60 degrees C, with an delta Hcal of 1058 +/- 59 kcal/mol. The melting of S-1 showed a single peak at 46.3 +/- 0.1 degrees C with an delta Hcal of 255 +/- 12 kcal/mol. Light chains melted at 51.0 +/- 0.2 degrees C with an delta Hcal of 85 +/- 15 kcal/mol.(ABSTRACT TRUNCATED AT 250 WORDS) Study holds ProTherm entries: 3926, 3927 Extra Details: additive : EDTA(1 mM), multistep endothermic proces; isolated fragments;,structural stability; endotherm

Submission Details

ID: 36RLMi7Z

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:23 p.m.

Version: 1

Publication Details
Bertazzon A;Tsong TY,Biochemistry (1989) High-resolution differential scanning calorimetric study of myosin, functional domains, and supramolecular structures. PMID:2611262
Additional Information

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
4QNH 2014-06-17T00:00:00+0000 2.02 Calcium-calmodulin (T79D) complexed with the calmodulin binding domain from a small conductance potassium channel SK2-a
6ALE 2017-08-07T00:00:00+0000 2.5 A V-to-F substitution in SK2 channels causes Ca2+ hypersensitivity and improves locomotion in a C. elegans ALS model
1OOJ 2003-03-03T00:00:00+0000 2.11 Structural genomics of Caenorhabditis elegans : Calmodulin
2LV6 2012-06-29T00:00:00+0000 0 The complex between Ca-Calmodulin and skeletal muscle myosin light chain kinase from combination of NMR and aqueous and contrast-matched SAXS data
2MES 2013-09-26T00:00:00+0000 0 Backbone 1H, 13C, 15N resonance assignments of calcium-bound calmodulin in complex with PSD95 N-terminal peptide
2RRT 2011-04-27T00:00:00+0000 0 Solution structure of Magnesium-bound form of calmodulin C-domain E104D/E140D mutant
3KF9 2009-10-27T00:00:00+0000 2.6 Crystal structure of the SdCen/skMLCK complex
5H7D 2016-11-17T00:00:00+0000 2.57 Crystal structure of the YgjG-protein A-Zpa963-calmodulin complex

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 B Calmodulin P20689 MYLK2_RAT
100.0 B Calmodulin P07313 MYLK2_RABIT
100.0 B Calmodulin Q8VCR8 MYLK2_MOUSE
100.0 B Calmodulin Q9H1R3 MYLK2_HUMAN
100.0 B Calmodulin A4IFM7 MYLK2_BOVIN
93.5 A Calmodulin P18061 CALM_TRYCR
93.5 A Calmodulin P69098 CALM_TRYBG
93.5 A Calmodulin P69097 CALM_TRYBB
100.0 A Calmodulin P62184 CALM_RENRE
100.0 A Calmodulin P11121 CALM_PYUSP
100.0 A Calmodulin P02595 CALM_PATSP
92.3 A Calmodulin P53440 CALMF_NAEGR
94.2 A Calmodulin P11118 CALM_EUGGR
100.0 A Calmodulin P02594 CALM_ELEEL
91.4 A Calmodulin P05932 CALMB_ARBPU
96.5 A Calmodulin Q9HFY6 CALM_BLAEM
100.0 A Calmodulin Q40302 CALM_MACPY
91.9 A Calmodulin P62150 CALM_ORYLA
95.7 A Calmodulin O02367 CALM_CIOIN
91.2 A Calmodulin P27166 CALM_STYLE
91.2 A Calmodulin O97341 CALM_SUBDO
91.2 A Calmodulin A8I1Q0 CALM_HETTR
92.6 A Calmodulin P02598 CALM_TETPY
92.6 A Calmodulin A3E4D8 CALM_PROMN
92.6 A Calmodulin A3E3H0 CALM_PFIPI
92.6 A Calmodulin A3E4F9 CALM_KARVE
92.6 A Calmodulin A4UHC0 CALM_ALEFU
92.6 A Calmodulin O96081 CALMB_HALRO
92.6 A Calmodulin P62146 CALMA_ARBPU
98.3 A Calmodulin Q95NR9 CALM_METSE
97.4 A Calmodulin Q7T3T2 CALM_EPIAK
98.3 A Calmodulin P0DP35 CAM2B_XENLA
98.3 A Calmodulin P0DP34 CAM2A_XENLA
98.3 A Calmodulin P62151 CALM_TETCF
98.3 A Calmodulin P21251 CALM_STIJA
98.3 A Calmodulin Q6YNX6 CALM_SHEEP
98.3 A Calmodulin P62160 CALM_RABIT
98.3 A Calmodulin Q5RAD2 CALM_PONAB
98.3 A Calmodulin Q71UH6 CALM_PERFV
98.3 A Calmodulin P62156 CALM_ONCSP
98.3 A Calmodulin Q6PI52 CALM_DANRE
98.3 A Calmodulin Q6IT78 CALM_CTEID
98.3 A Calmodulin P62149 CALM_CHICK
98.3 A Calmodulin P62157 CALM_BOVIN
98.3 A Calmodulin P62144 CALM_ANAPL
98.3 A Calmodulin P0DP31 CALM3_RAT
98.3 A Calmodulin P0DP28 CALM3_MOUSE
98.3 A Calmodulin P0DP25 CALM3_HUMAN
98.3 A Calmodulin P0DP30 CALM2_RAT
98.3 A Calmodulin P0DP27 CALM2_MOUSE
98.3 A Calmodulin P0DP24 CALM2_HUMAN
99.1 A Calmodulin Q9UB37 CALM2_BRALA
98.3 A Calmodulin P0DP33 CALM1_XENLA
98.3 A Calmodulin P0DP29 CALM1_RAT
98.3 A Calmodulin P0DP26 CALM1_MOUSE
98.3 A Calmodulin P0DP23 CALM1_HUMAN
98.0 A Calmodulin Q8STF0 CALM_STRIE
99.3 A Calmodulin P62154 CALM_LOCMI
99.3 A Calmodulin P62152 CALM_DROME
99.3 A Calmodulin P62145 CALM_APLCA
99.3 A Calmodulin P62153 CALMA_HALRO
99.3 A Calmodulin P62148 CALM1_BRALA
99.3 A Calmodulin P62147 CALM1_BRAFL
98.6 A Calmodulin O16305 CALM_CAEEL