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Items: 1 to 20 of 180

1.

Molten globule and protein folding.

Ptitsyn OB.

Adv Protein Chem. 1995;47:83-229. Review. No abstract available.

PMID:
8561052
2.
4.
5.

Effects of amino acid substitutions in the hydrophobic core of alpha-lactalbumin on the stability of the molten globule state.

Uchiyama H, Perez-Prat EM, Watanabe K, Kumagai I, Kuwajima K.

Protein Eng. 1995 Nov;8(11):1153-61.

PMID:
8819981
6.

Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway.

Cavagnero S, Nishimura C, Schwarzinger S, Dyson HJ, Wright PE.

Biochemistry. 2001 Dec 4;40(48):14459-67.

PMID:
11724558
8.

Protein folding. Solid evidence for molten globules.

Dobson CM.

Curr Biol. 1994 Jul 1;4(7):636-40. Review.

PMID:
7953543
9.
10.

Structure and dynamics of the alpha-lactalbumin molten globule: fluorescence studies using proteins containing a single tryptophan residue.

Chakraborty S, Ittah V, Bai P, Luo L, Haas E, Peng Z.

Biochemistry. 2001 Jun 19;40(24):7228-38.

PMID:
11401570
12.
13.

Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy.

Mizuguchi M, Arai M, Ke Y, Nitta K, Kuwajima K.

J Mol Biol. 1998;283(1):265-77.

PMID:
9761689
14.

Leishmania donovani trypanothione reductase: role of urea and guanidine hydrochloride in modulation of functional and structural properties.

Rai S, Dwivedi UN, Goyal N.

Biochim Biophys Acta. 2009 Oct;1794(10):1474-84. doi: 10.1016/j.bbapap.2009.06.017. Epub 2009 Jun 27.

PMID:
19563920
15.
17.

Stabilization of molten globule state of papain by urea.

Edwin F, Sharma YV, Jagannadham MV.

Biochem Biophys Res Commun. 2002 Feb 8;290(5):1441-6.

PMID:
11820783
18.
19.

Which came first, protein sequence or structure?

Karkar M.

Science. 1996 Aug 2;273(5275):610. No abstract available.

PMID:
8701315
20.

An NMR view of the folding process of a CheY mutant at the residue level.

Garcia P, Serrano L, Rico M, Bruix M.

Structure. 2002 Sep;10(9):1173-1185.

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