α-lactalbumin: compact state with fluctuating tertiary structure?
作者： D.A. Dolgikh , R.I. Gilmanshin , E.V. Brazhnikov , V.E. Bychkova , G.V. Semisotnov
DOI: 10.1016/0014-5793(81)80642-4
关键词:
摘要: Gu-HCl shows a non-simultaneous change of different optical properties: the CD spectrum in near UV (aromatic) region changes at smaller concentrations than far (peptide) [l--4]. This suggests existence stable, partly denatured (intermediate) forms these proteins with more or less symmetrical environment aromatic groups but native-like secondary structure. For both bovine [2] and human [4] a-lactalbumins as well for some other [S] similar state exists also acid pH. While (P) form moderate usually can be obtained only mixture native (N) and/or unfolded (U) forms, (A) studied pure state. It was shown that (u-LA U + A transition takes
core.ac.uk
elsevier.com
sci-hub.se 参考文章(20)
Kin-Ping Wong, Charles Tanford, Denaturation of Bovine Carbonic Anhydrase B by Guanidine Hydrochloride A PROCESS INVOLVING SEPARABLE SEQUENTIAL CONFORMATIONAL TRANSITIONS Journal of Biological Chemistry. ,vol. 248, pp. 8518- 8523 ,(1973) , 10.1016/S0021-9258(19)43163-3
R W Henkens, P J Stein, Detection of intermediates in protein folding of carbonic anhydrase with fluorescence emission and polarization. Journal of Biological Chemistry. ,vol. 253, pp. 8016- 8018 ,(1978) , 10.1016/S0021-9258(17)34354-5
Shingo Kato, Motoyoshi Okamura, Nobuo Shimamoto, Hiroyasu Utiyama, Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme. Biochemistry. ,vol. 20, pp. 1080- 1085 ,(1981) , 10.1021/BI00508A006
Makoto Nozaka, Kunihiro Kuwajima, Katsutoshi Nitta, Shintaro Sugai, Detection and characterization of the intermediate on the folding pathway of human alpha-lactalbumin. Biochemistry. ,vol. 17, pp. 3753- 3758 ,(1978) , 10.1021/BI00611A013
V. S. Ananthanarayanan, F. Ahmad, Evidence from rotatory measurements for an intermediate state in the guanidine hydrochloride denaturation of β-lactoglobulin Canadian Journal of Biochemistry. ,vol. 55, pp. 239- 243 ,(1977) , 10.1139/O77-033
Kunihiro Kuwajima, A folding model of α-lactalbumin deduced from the three-state denaturation mechanism Journal of Molecular Biology. ,vol. 114, pp. 241- 258 ,(1977) , 10.1016/0022-2836(77)90208-X
L.V. Abaturov, N.N. Yakobashvily, K.Sh. Jinoria, T.P. Molchanova, Ya.M. Varshavsky, Effect of inter-subunit contact on intramolecular conformational motility (conformational stability) of hemoglobin as revealed by hydrogen exchange FEBS Letters. ,vol. 70, pp. 127- 130 ,(1976) , 10.1016/0014-5793(76)80741-7
Kunihiro Kuwajima, Katsutoshi Nitta, Michio Yoneyama, Shintaro Sugai, Three-state denaturation of α-lactalbumin by guanidine hydrochloride Journal of Molecular Biology. ,vol. 106, pp. 359- 373 ,(1976) , 10.1016/0022-2836(76)90091-7
J. McD. Armstrong, K.E. Hopper, H.A. McKenzie, W.H. Murphy, On the column chromatography of bovine whey proteins Biochimica et Biophysica Acta (BBA) - Protein Structure. ,vol. 214, pp. 419- 426 ,(1970) , 10.1016/0005-2795(70)90300-4
K. H. Cook, F. X. Schmid, R. L. Baldwin, Role of proline isomerization in folding of ribonuclease A at low temperatures. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 76, pp. 6157- 6161 ,(1979) , 10.1073/PNAS.76.12.6157