The Use of Synthetic Peptides to Unravel the Mechanism of Muscle Regulation

Jennifer E. Van Eyk, Robert S. Hodges

Research output: Contribution to journalArticle

Abstract

Synthetic peptides have been used successfully as probes in studying the relationship between protein structure and function. The biological and functionally important regions of three muscle proteins, troponin C, troponin I, and actin, are presented in this review. The small size of these peptides has enabled the determination of their free or bound structures by two-dimensional or trNOE NMR techniques. These biological and structural results have greatly advanced our understanding of the complex protein-protein interactions involved in muscle regulation. These studies emphasize that small synthetic peptides can mimic the biological activity of their native protein and that small linear sequences are important molecular recognition sites in protein-protein interactions. In addition, three-dimensional structural information is still inherent in the amino acid sequence of these peptides.

Original languageEnglish (US)
Pages (from-to)264-280
Number of pages17
JournalMethods
Volume5
Issue number3
DOIs
StatePublished - Dec 1993
Externally publishedYes

Fingerprint

Muscle
Muscles
Peptides
Proteins
Troponin C
Molecular recognition
Troponin I
Muscle Proteins
Protein C
Bioactivity
Actins
Amino Acid Sequence
Nuclear magnetic resonance
Amino Acids

ASJC Scopus subject areas

  • Molecular Biology

Cite this

The Use of Synthetic Peptides to Unravel the Mechanism of Muscle Regulation. / Van Eyk, Jennifer E.; Hodges, Robert S.

In: Methods, Vol. 5, No. 3, 12.1993, p. 264-280.

Research output: Contribution to journalArticle

Van Eyk, Jennifer E. ; Hodges, Robert S. / The Use of Synthetic Peptides to Unravel the Mechanism of Muscle Regulation. In: Methods. 1993 ; Vol. 5, No. 3. pp. 264-280.
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