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Circular dichroism of the “random” polypeptide chain
Open accessAbstract
The circular dichroism (CD) spectrum of an unordered polypeptide chain does not correspond, as has been assumed heretofore, to that of a charged chain such as poly‐L‐glutamic acid or poly‐L‐lysine. The latter have been shown to have locally ordered structures with characteristic CD spectra. We have now obtained CD spectra of the unordered forms of the above synthetic, polypeptides, as well as of two fibrous proteins (collagen and feather keratin) and a globular protein (myoglobin). These spectra are all similar to that of unordered polyproline, having a negative band in the vicinity of 2000 mμ and no additional bands at longer wavelengths. The lack of structural uniqueness of the unordered polypeptide chain is emphasized by these studies.
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Cited by
[27] Circular dichroism and optical rotatory dispersion of proteins and polypeptides
Adler, A. J., Greenfield, N. J., & Fasman, G. D. (1973) · Methods in Enzymology · doi:10.1016/s0076-6879(73)27030-1 · Cited by 553
Poly-γ-glutamic acid: production, properties and applications
Ogunleye, A., Bhat, A., Irorere, V. U., Hill, D., Williams, C., & Radecka, I. (2015) · Microbiology · doi:10.1099/mic.0.081448-0 · Cited by 354
The pH-dependent bilayer destabilization by an amphipathic peptide
Subbarao, N. K., Parente, R. A., Szoka, F. C., Nadasdi, L., & Pongracz, K. (1987) · Biochemistry · doi:10.1021/bi00385a002 · Cited by 295
Dukor, R. K., & Keiderling, T. A. (1991) · Biopolymers · doi:10.1002/bip.360311409 · Cited by 264
Lee, S., Müller, M., Rezwan, K., & Spencer, N. D. (2005) · Langmuir · doi:10.1021/la050779w · Cited by 173
Metadata
- Authors
- Tiffany, M. L., & Krimm, S.
- Venue
- Biopolymers
- Publisher
- Wiley
- Published
- 1969-09
- Volume
- 8
- Issue
- 3
- Pages
- 347-359
- ISSN
- 0006-3525 (ISSN-L)
- 1097-0282
- OpenAlex
- W2129064469
- Cited by
- 268
- References
- 0
- FWCI
- 8.90
- Type
- journal article
- Language
- en
- Open access
- green
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