DOI: 10.1002/bip.1972.360111210. Raman scattering of chymotrypsinogen A, ribonuclease, and ovalbumin in the aqueous solution and solid state

Raman scattering of chymotrypsinogen A, ribonuclease, and ovalbumin in the aqueous solution and solid state

10.1002/bip.1972.360111210

Crossref journal-article

Wiley

Biopolymers (311)

Abstract

AbstractThe Raman spectra of three globular proteins, beef pancreas chymotrypsinogen A, beef pancreas ribonuclease, and hen egg white ovalbumin have been obtained in the solid state and aqueous solution. X‐ray diffraction and circular dichroism evidence have indicated that these proteins have a low α‐helical content and a large fraction of the residues in the unordered and β‐sheet conformation. The frequencies and intensities of the amide I and amide III lines are consistent with assignments based on the Raman spectra of polypeptides. The intense amide III lines observed in all the spectra would be expected for proteins with a low fraction of the residues in the α‐helical conformation. Several spectra changes occur upon dissolution of the proteins in water and may be associated with further hydration of the proteins. The spectrum of thermally denatured chymotrypsinogen is presented. A 3 cm–1 decrease in the frequency of the amide I line of the protein dissolved in D2O upon heating was observed. This observation is consistent with a denaturation mechanism allowing only slight changes in the secondary structure but an increase in solvent penetration upon going from the native to the reversibly denatured state.

Bibliography

Koenig, J. L., & Frushour, B. G. (1972). Raman scattering of chymotrypsinogen A, ribonuclease, and ovalbumin in the aqueous solution and solid state. Biopolymers, 11(12), 2505â2520. Portico.

Authors 2

J. L. Koenig (first)
B. G. Frushour (additional)

References 31 Referenced 32

10.1016/S0065-3233(08)60401-5
{'key': 'e_1_2_1_3_2', 'volume-title': 'Mechanism in Protein Denaturation', 'author': 'Jolly M.', 'year': '1964'} / Mechanism in Protein Denaturation by Jolly M. (1964)
10.1016/0022-2836(70)90208-1
10.1126/science.161.3836.68
10.1007/BF02196195
{'key': 'e_1_2_1_7_2', 'volume-title': 'Structure and Stability of Biological Macromolecules', 'author': 'Brandts J. F.', 'year': '1969'} / Structure and Stability of Biological Macromolecules by Brandts J. F. (1969)
10.1093/oxfordjournals.jbchem.a128138 / J. Biochem. by Hamaguchi K. (1965)
Koenig J. L. J. Polym. Sci. C in press.
{'key': 'e_1_2_1_10_2', 'first-page': '449', 'volume-title': 'The Proteins', 'author': 'Weber G.', 'year': '1965'} / The Proteins by Weber G. (1965)
{'key': 'e_1_2_1_11_2', 'first-page': '593', 'volume-title': 'Structure and Stability of Biological Macromolecules', 'author': 'Susi H.', 'year': '1969'} / Structure and Stability of Biological Macromolecules by Susi H. (1969)
E.Blout personal communication.
10.1080/05704927108082605
10.1063/1.1673659
10.1101/SQB.1938.006.01.006
10.1085/jgp.34.5.583
{'key': 'e_1_2_1_17_2', 'volume-title': 'Structure and Stability of Biological Macromolecules', 'author': 'Lumry R. L.', 'year': '1969'} / Structure and Stability of Biological Macromolecules by Lumry R. L. (1969)
10.1021/ja01074a013
10.1021/ja01074a014
10.1021/bi00890a004
{'key': 'e_1_2_1_21_2', 'first-page': '7259', 'volume': '91', 'author': 'Koenig J. L.', 'year': '1969', 'journal-title': 'J. Amer. Chem. Soc.'} / J. Amer. Chem. Soc. by Koenig J. L. (1969)
J. L.KoenigandB. F.Frushour unpublished data.
10.1016/0022-2836(70)90137-3
10.1021/ja00983a001
10.1002/bip.360100108
10.1073/pnas.58.1.304
{'key': 'e_1_2_1_27_2', 'first-page': '486', 'volume': '16', 'author': 'Urnes P.', 'year': '1961', 'journal-title': 'Advan. Protein. Chem.'} / Advan. Protein. Chem. by Urnes P. (1961)
10.1002/bip.1969.360080203
10.1038/213862a0
10.1021/bi00838a031
Kon HoCho The Conformation and Denaturation of Ovalbumin Ph.D. Thesis Princeton University 1970.
10.1021/ja00761a069

Dates

Type	When
Created	20 years, 8 months ago (Dec. 30, 2004, 11:22 p.m.)
Deposited	1 year, 9 months ago (Nov. 11, 2023, 10:57 p.m.)
Indexed	1 year, 9 months ago (Nov. 23, 2023, 7:44 a.m.)
Issued	52 years, 9 months ago (Dec. 1, 1972)
Published	52 years, 9 months ago (Dec. 1, 1972)
Published Online	21 years, 7 months ago (Feb. 1, 2004)
Published Print	52 years, 9 months ago (Dec. 1, 1972)

Funders 0

None

BibTeX

@article{Koenig_1972, title={Raman scattering of chymotrypsinogen A, ribonuclease, and ovalbumin in the aqueous solution and solid state}, volume={11}, ISSN={1097-0282}, url={http://dx.doi.org/10.1002/bip.1972.360111210}, DOI={10.1002/bip.1972.360111210}, number={12}, journal={Biopolymers}, publisher={Wiley}, author={Koenig, J. L. and Frushour, B. G.}, year={1972}, month=dec, pages={2505–2520} }

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