Identification of Beta,beta-turns and Unordered Conformations in Polypeptide Chains by Vacuum Ultraviolet Circular Dichroism

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1977 Aug 1

PMID 269385

Citations 22

Authors

S BRAHMS

J Brahms

G SPACH

A Brack

Affiliations

Soon will be listed here.

Abstract

Different conformations of polypeptides were characterized by measurements of the circular dichroism (CD) extended into the vacuum ultraviolet region. (i) The linear beta-pleated sheet structure was characterized in a broad ultraviolet region down to 165 nm by examination of copolypeptides composed of alternating hydrophobic and hydrophilic amino-acid residues, e.g., poly(Lys-Leu-Lys-Leu). A short-wavelength intense band was found at about 169 nm, which is characteristic of beta-pleated sheet conformation. (ii) The beta-turns were experimentally measured using poly(Ala(2)-Gly(2)) in a broad spectral region down to 165 nm with accuracy. The observed CD spectrum is in excellent qualitative agreement with the theoretical curve calculated by Woody for the beta-turns of type II and/or I of Venkatachalam. The similarity in shape between the theoretical curve and the observed CD spectra suggests a dominance of beta-turn segments in the poly(Ala(2)-Gly(2)) structure. The presence of beta-turns in poly(Ala(2)-Gly(2)) is also in agreement with the characterization of this polypeptide by solid state methods (electron microscopy and x-ray diffraction). The CD spectrum of beta-turns is characterized by a very intense band at 207.5 nm and strong negative bands at 191 and 169 nm. Copolypeptides such as poly(Ala(2)-Gly(3)) and poly(Ala(3)-Gly(3)) yielded a similar type of CD spectrum, analysis of which indicates that a large fraction of their residues is contained in beta-turn regions. (iii) The CD spectrum of the unordered chain of these alternating copolypeptides in salt-free solution is observed in the vacuum ultraviolet region.

Citing Articles

Functional and Biochemical Analyses of Glycerol Kinase and Glycerol 3-phosphate Dehydrogenase in HEK293 Cells.

Syngkli S, Singh S, Rani R, Das B Protein J. 2025; .

PMID: 39987391 DOI: 10.1007/s10930-025-10252-1.

Thermotolerance Mechanism of Fungal GH6 Cellobiohydrolase. Part I. Characterization of Thermotolerant Mutant from the Basidiomycete .

Yamaguchi S, Sunagawa N, Samejima M, Igarashi K J Appl Glycosci (1999). 2024; 71(2):55-62.

PMID: 38863951 PMC: 11163330. DOI: 10.5458/jag.jag.JAG-2023_0017.

Interactions of Nanoscale Self-Assembled Peptide-Based Assemblies with Glioblastoma Cell Models and Spheroids.

Lebedenko C, Murray M, Goncalves B, Perez D, Lambo D, Banerjee I ACS Omega. 2023; 8(13):12124-12143.

PMID: 37033803 PMC: 10077566. DOI: 10.1021/acsomega.2c08049.

The Impact of Tyrosine Iodination on the Aggregation and Cleavage Kinetics of MMP-9-Responsive Peptide Sequences.

MacPherson D, McPhee S, Zeglis B, Ulijn R ACS Biomater Sci Eng. 2022; 8(2):579-587.

PMID: 35050574 PMC: 9153392. DOI: 10.1021/acsbiomaterials.1c01488.

The Aβ(1-38) peptide is a negative regulator of the Aβ(1-42) peptide implicated in Alzheimer disease progression.

Quartey M, Nyarko J, Maley J, Barnes J, Bolanos M, Heistad R Sci Rep. 2021; 11(1):431.

PMID: 33432101 PMC: 7801637. DOI: 10.1038/s41598-020-80164-w.

References

Holzwarth G, Doty P . THE ULTRAVIOLET CIRCULAR DICHROISM OF POLYPEPTIDES. J Am Chem Soc. 1965; 87:218-28. DOI: 10.1021/ja01080a015. View

Chou P, Fasman G . Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry. 1974; 13(2):211-22. DOI: 10.1021/bi00699a001. View

Venkatachalam C . Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units. Biopolymers. 1968; 6(10):1425-36. DOI: 10.1002/bip.1968.360061006. View

Chen Y, Yang J, Chau K . Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry. 1974; 13(16):3350-9. DOI: 10.1021/bi00713a027. View

Jenness D, Sprecher C, Johnson Jr W . Circular dichroism of collagen, gelatin, and poly(proline) II in the vacuum ultraviolet. Biopolymers. 1976; 15(3):513-21. DOI: 10.1002/bip.1976.360150308. View

Brack A, Orgel L . Beta structures of alternating polypeptides and their possible prebiotic significance. Nature. 1975; 256(5516):383-7. DOI: 10.1038/256383a0. View

Crawford J, Lipscomb W, SCHELLMAN C . The reverse turn as a polypeptide conformation in globular proteins. Proc Natl Acad Sci U S A. 1973; 70(2):538-42. PMC: 433301. DOI: 10.1073/pnas.70.2.538. View

Urry D, Long M, Ohnishi T, Jacobs M . Circular dichroism and absorption of the polytetrapeptide of elastin: a polymer model for the beta-turn. Biochem Biophys Res Commun. 1974; 61(4):1427-33. DOI: 10.1016/s0006-291x(74)80442-0. View

Lotz B, Brack A, SPACH G . Beta structure of periodic copolypeptides of L-alanine and glycine. Their relevance to the structure of silks. J Mol Biol. 1974; 87(2):193-203. DOI: 10.1016/0022-2836(74)90143-0. View

10.

Chothia C . Conformation of twisted beta-pleated sheets in proteins. J Mol Biol. 1973; 75(2):295-302. DOI: 10.1016/0022-2836(73)90022-3. View

11.

TIFFANY M, Krimm S . Effect of temperature on the circular dichroism spectra of polypeptides in the extended state. Biopolymers. 1972; 11(11):2309-16. DOI: 10.1002/bip.1972.360111109. View

12.

Johnson Jr W, Tinoco Jr I . Circular dichroism of polypeptide solutions in the vacuum ultraviolet. J Am Chem Soc. 1972; 94(12):4389-92. DOI: 10.1021/ja00767a084. View

13.

Madison V, SCHELLMAN J . Optical activity of polypeptides and proteins. Biopolymers. 1972; 11(5):1041-76. DOI: 10.1002/bip.1972.360110509. View

14.

Brack A, SPACH G . Synthesis and conformations of periodic copolypeptides of L-alanine and Glycine. Biopolymers. 1972; 11(3):563-86. DOI: 10.1002/bip.1972.360110304. View

15.

Lewis P, Momany F, Scheraga H . Folding of polypeptide chains in proteins: a proposed mechanism for folding. Proc Natl Acad Sci U S A. 1971; 68(9):2293-7. PMC: 389403. DOI: 10.1073/pnas.68.9.2293. View

16.

Balcerski J, Pysh E, Bonora G, Toniolo C . Vacuum ultraviolet circular dichroism of beta-forming alkyl oligopeptides. J Am Chem Soc. 1976; 98(12):3470-3. DOI: 10.1021/ja00428a013. View

17.

Baker C, Isenberg I . On the analysis of circular dichroic spectra of proteins. Biochemistry. 1976; 15(3):629-34. DOI: 10.1021/bi00648a028. View

18.

Kubota S, Fasman G . The beta conformation of polypeptides of valine, isoleucine, and threonine in solution and solid-state: optical and infrared studies. Biopolymers. 1975; 14(3):605-31. DOI: 10.1002/bip.1975.360140314. View

19.

Sarkar P, Doty P . The optical rotatory properties of the beta-configuration in polypeptides and proteins. Proc Natl Acad Sci U S A. 1966; 55(4):981-9. PMC: 224260. DOI: 10.1073/pnas.55.4.981. View

20.

IIZUKA E, Yang J . Optical rotatory dispersion and circular dichroism of the beta-form of silk fibroin in solution. Proc Natl Acad Sci U S A. 1966; 55(5):1175-82. PMC: 224296. DOI: 10.1073/pnas.55.5.1175. View