Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry.


Abstract

Differential scanning calorimetry (DSC) was employed for studying the thermal unfolding of myosin and its rod part prepared from carp acclimated to 10 and 30 degrees C. Differences in the thermal stability reflecting structural properties were clearly demonstrated by the DSC data obtained at pH 8.0 in 0.6 M KCl for the two types of carp myosin and rod. The transition temperatures on myosin and rod given by the major peaks for the 10 degrees C-acclimated carp were 33.9 and 47.4 degrees C and 33.0 and 44.0 degrees C, respectively, assuming two endotherms for this type. Since the shape of the first peaks at 33.9 and 33.0 degrees C was not symmetrical, two peaks having similar transition temperatures overlapped in this temperature range. When the data were analyzed using three endotherms, the three transition temperatures obtained for myosin and rod were 32.8, 34.9, and 47.4 degrees C and 32.9, 33.4, and 44.1 degrees C, respectively. Thus, the position of the first peak for the 10 degrees C-acclimated carp myosin did not change even after removal of the large subfragment-1 part, but the transition of the second peak shifted to a lower temperature by about 3 degrees C. The myosin and rod from carp acclimated to 30 degrees C showed three distinct peaks at 35.9, 39.7, and 49.1 degrees C and 34.5, 39.7, and 46.7 degrees C, respectively. The position of the largest peak for myosin remained unchanged, and the shift of the peak position of the highest temperature was about 3 degrees C, as obtained for the 10 degrees C-acclimated carp.(ABSTRACT TRUNCATED AT 250 WORDS) Study holds ProTherm entries: 4728, 4729, 4730, 4731, 4732, 4733, 4734, 4735, 4736, 4737, 4738, 4739, 4740, 4741, 4742, 4743, 4744, 4745, 4746, 4747, 4748, 4749, 4750, 4751, 4752, 4753, 4754, 4755 Extra Details: transition 1; 10 degrees C acclimated structural properties; endotherms; acclimated rod;,alpha-helices

Submission Details

ID: 6cKnoziF4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:27 p.m.

Version: 1

Publication Details
Nakaya M;Watabe S;Ooi T,Biochemistry (1995) Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry. PMID:7893723
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
5KHT 2017-06-21 1.5 Crystal structure of the N-terminal fragment of tropomyosin isoform Tpm1.1 at 1.5 A resolution
3U1C 2011-11-23 1.8 Anti-parallel dimer of N-terminal 98-aa fragment of smooth muscle tropomyosin alpha
1IC2 2001-07-25 2.0 DECIPHERING THE DESIGN OF THE TROPOMYOSIN MOLECULE
3U1A 2011-11-23 2.0 N-terminal 81-aa fragment of smooth muscle tropomyosin alpha
3MTU 2010-06-23 2.1 Structure of the Tropomyosin Overlap Complex from Chicken Smooth Muscle
3MUD 2010-06-23 2.2 Structure of the Tropomyosin Overlap Complex from Chicken Smooth Muscle

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Tropomyosin alpha-1 chain A1XQV4 TPM3_PIG
100.0 Tropomyosin alpha-1 chain P06753 TPM3_HUMAN
100.0 Tropomyosin alpha-1 chain Q5KR47 TPM3_BOVIN
100.0 Tropomyosin alpha-1 chain Q01173 TPM1_XENLA
100.0 Tropomyosin alpha-1 chain P13105 TPM1_RANTE
100.0 Tropomyosin alpha-1 chain P09493 TPM1_HUMAN
100.0 Tropomyosin alpha-1 chain P13104 TPM1_DANRE
100.0 Tropomyosin alpha-1 chain P58773 TPM1_COTJA
100.0 Tropomyosin alpha-1 chain P04268 TPM1_CHICK
100.0 Tropomyosin alpha-1 chain P84335 TPM1_CHEAU