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 language | English (US) |
|---|---|
| Pages (from-to) | 264-280 |
| Number of pages | 17 |
| Journal | Methods |
| Volume | 5 |
| Issue number | 3 |
| DOIs | |
| State | Published - Dec 1993 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - The Use of Synthetic Peptides to Unravel the Mechanism of Muscle Regulation
AU - Van Eyk, Jennifer E.
AU - Hodges, Robert S.
PY - 1993/12
Y1 - 1993/12
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0000290298&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0000290298&partnerID=8YFLogxK
U2 - 10.1006/meth.1993.1033
DO - 10.1006/meth.1993.1033
M3 - Article
AN - SCOPUS:0000290298
VL - 5
SP - 264
EP - 280
JO - ImmunoMethods
JF - ImmunoMethods
SN - 1046-2023
IS - 3
ER -