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Items: 1 to 20 of 115

1.

Delineation of solution burst-phase protein folding events by encapsulating the proteins in silica gels.

Okabe T, Tsukamoto S, Fujiwara K, Shibayama N, Ikeguchi M.

Biochemistry. 2014 Jun 17;53(23):3858-66. doi: 10.1021/bi5003647. Epub 2014 Jun 5.

PMID:
24867232
2.

Non-native alpha-helix formation is not necessary for folding of lipocalin: comparison of burst-phase folding between tear lipocalin and beta-lactoglobulin.

Tsukamoto S, Yamashita T, Yamada Y, Fujiwara K, Maki K, Kuwajima K, Matsumura Y, Kihara H, Tsuge H, Ikeguchi M.

Proteins. 2009 Jul;76(1):226-36. doi: 10.1002/prot.22340. Erratum in: Proteins. 2009 Dec;77(4):1015.

PMID:
19137619
3.
4.

Kinetic and equilibrium intermediate states are different in LYLA1, a chimera of lysozyme and alpha-lactalbumin.

Haezebrouck P, Noyelle K, Joniau M, Van Dael H.

J Mol Biol. 1999 Oct 29;293(3):703-18.

PMID:
10543961
5.

Cooperative folding of the isolated alpha-helical domain of hen egg-white lysozyme.

Bai P, Peng Z.

J Mol Biol. 2001 Nov 23;314(2):321-9.

PMID:
11718563
6.
7.

A circumventing role for the non-native intermediate in the folding of β-lactoglobulin.

Sakurai K, Fujioka S, Konuma T, Yagi M, Goto Y.

Biochemistry. 2011 Jul 26;50(29):6498-507. doi: 10.1021/bi200241a. Epub 2011 Jun 30.

PMID:
21678970
8.
9.

Conserved folding pathways of alpha-lactalbumin and lysozyme revealed by kinetic CD, fluorescence, NMR, and interrupted refolding experiments.

Schlepckow K, Wirmer J, Bachmann A, Kiefhaber T, Schwalbe H.

J Mol Biol. 2008 May 2;378(3):686-98. doi: 10.1016/j.jmb.2008.02.033. Epub 2008 Feb 29.

PMID:
18377934
10.

Effects of a helix substitution on the folding mechanism of bovine alpha-lactalbumin.

Mizuguchi M, Kobashigawa Y, Kumaki Y, Demura M, Kawano K, Nitta K.

Proteins. 2002 Oct 1;49(1):95-103.

PMID:
12211019
11.

Equilibrium and kinetic folding of hen egg-white lysozyme under acidic conditions.

Sasahara K, Demura M, Nitta K.

Proteins. 2002 Dec 1;49(4):472-82.

PMID:
12402357
12.

Folding of lysozyme.

Fischer B.

EXS. 1996;75:143-61. Review.

PMID:
8765299
13.

Slow motion analysis of protein folding intermediates within wet silica gels.

Shibayama N.

Biochemistry. 2008 May 27;47(21):5784-94. doi: 10.1021/bi8003582. Epub 2008 May 1.

PMID:
18447365
14.

Circular dichroism of protein-folding intermediates.

Woody RW.

Methods Enzymol. 2004;380:242-85. No abstract available.

PMID:
15051341
15.
16.

Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy.

Arai M, Ikura T, Semisotnov GV, Kihara H, Amemiya Y, Kuwajima K.

J Mol Biol. 1998 Jan 9;275(1):149-62.

PMID:
9451446
17.

Circular dichroism study on the early folding events of beta-lactoglobulin entrapped in wet silica gels.

Shibayama N.

FEBS Lett. 2008 Jul 23;582(17):2668-72. doi: 10.1016/j.febslet.2008.06.047. Epub 2008 Jun 30.

18.
19.

Protein dissection experiments reveal key differences in the equilibrium folding of alpha-lactalbumin and the calcium binding lysozymes.

Chowdhury FA, Fairman R, Bi Y, Rigotti DJ, Raleigh DP.

Biochemistry. 2004 Aug 10;43(31):9961-7.

PMID:
15287723
20.

Different folding pathways taken by highly homologous proteins, goat alpha-lactalbumin and canine milk lysozyme.

Nakamura T, Makabe K, Tomoyori K, Maki K, Mukaiyama A, Kuwajima K.

J Mol Biol. 2010 Mar 12;396(5):1361-78. doi: 10.1016/j.jmb.2010.01.021. Epub 2010 Jan 18.

PMID:
20080106

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