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PMID: 8343116 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Studies on secondary structure of caldesmon and its C-terminal fragments.

The Biochemical journal ·Vol. 293 ( Pt 2) ·1993-07-15 ·Pages 363-8

Czuryło EA, Venyaminov SYu, Dabrowska R

Abstract

Evaluation of the secondary structure of caldesmon from c.d. spectra revealed that it contains 51% helix, 9% beta-strand and 40% of remainder structures. These values agree well with the predicted ones from amino acid sequence, assuming an extended chain structure for caldesmon. The estimates of the secondary-structure elements in C-terminal 34 kDa and 19 kDa fragments are: 11 and 12% helix, 22 and 20% beta-strand, 13 and 17% beta-turns and loops, and 54 and 50% of remainder structure respectively. The best fit of experimental data was obtained assuming the globular state of the fragments. On the basis of structural analysis and fragmentation by proteolytic and chemical cleavages the six-domain model of caldesmon is proposed.

MeSH Terms
Animals Calmodulin-Binding Proteins/chemistry Chickens Circular Dichroism Peptide Fragments/chemistry Protein Structure, Secondary Spectrophotometry, Ultraviolet
Chemicals
Calmodulin-Binding Proteins Peptide Fragments
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Czuryło E A
Nencki Institute of Experimental Biology, Department of Muscle Biochemistry, Warszawa, Poland.
Venyaminov SYu
Dabrowska R
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2930363
Published
1993-07-15
Pages
363-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1134368
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2930363 PMC Full Text View journal details
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