338 related articles for article (PubMed ID: 16121399)
41. A specific hydrophobic core in the alpha-lactalbumin molten globule.
Wu LC; Kim PS
J Mol Biol; 1998 Jul; 280(1):175-82. PubMed ID: 9653040
[TBL] [Abstract][Full Text] [Related]
42. Probing subtle differences in the hydrogen exchange behavior of variants of the human alpha-lactalbumin molten globule using mass spectrometry.
Last AM; Schulman BA; Robinson CV; Redfield C
J Mol Biol; 2001 Aug; 311(4):909-19. PubMed ID: 11518539
[TBL] [Abstract][Full Text] [Related]
43. Unfolding and refolding pathways of a major kinetic trap in the oxidative folding of alpha-lactalbumin.
Salamanca S; Chang JY
Biochemistry; 2005 Jan; 44(2):744-50. PubMed ID: 15641801
[TBL] [Abstract][Full Text] [Related]
44. Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: a (19)F-NMR study.
Bai P; Luo L; Peng Zy
Biochemistry; 2000 Jan; 39(2):372-80. PubMed ID: 10630998
[TBL] [Abstract][Full Text] [Related]
45. Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin.
Alexandrescu AT; Ng YL; Dobson CM
J Mol Biol; 1994 Jan; 235(2):587-99. PubMed ID: 8289283
[TBL] [Abstract][Full Text] [Related]
46. 1,1,1,3,3,3-hexafluoroisopropanol induced thermal unfolding and molten globule state of bovine alpha-lactalbumin: calorimetric and spectroscopic studies.
Kundu A; Kishore N
Biopolymers; 2004 Mar; 73(4):405-20. PubMed ID: 14991658
[TBL] [Abstract][Full Text] [Related]
47. Localized nature of the transition-state structure in goat alpha-lactalbumin folding.
Saeki K; Arai M; Yoda T; Nakao M; Kuwajima K
J Mol Biol; 2004 Aug; 341(2):589-604. PubMed ID: 15276846
[TBL] [Abstract][Full Text] [Related]
48. Hydrophobic sequence minimization of the alpha-lactalbumin molten globule.
Wu LC; Kim PS
Proc Natl Acad Sci U S A; 1997 Dec; 94(26):14314-9. PubMed ID: 9405609
[TBL] [Abstract][Full Text] [Related]
49. Contribution of individual residues to formation of the native-like tertiary topology in the alpha-lactalbumin molten globule.
Song J; Bai P; Luo L; Peng ZY
J Mol Biol; 1998 Jul; 280(1):167-74. PubMed ID: 9653039
[TBL] [Abstract][Full Text] [Related]
50. Calcium binding peptides from alpha-lactalbumin: implications for protein folding and stability.
Kuhlman B; Boice JA; Wu WJ; Fairman R; Raleigh DP
Biochemistry; 1997 Apr; 36(15):4607-15. PubMed ID: 9109670
[TBL] [Abstract][Full Text] [Related]
51. Solution structure of a peptide fragment of human alpha-lactalbumin in trifluoroethanol: a model for local structure in the molten globule.
Smith LJ; Alexandrescu AT; Pitkeathly M; Dobson CM
Structure; 1994 Aug; 2(8):703-12. PubMed ID: 7994570
[TBL] [Abstract][Full Text] [Related]
52. Stabilization of protein by replacement of a fluctuating loop: structural analysis of a chimera of bovine alpha-lactalbumin and equine lysozyme.
Tada M; Kobashigawa Y; Mizuguchi M; Miura K; Kouno T; Kumaki Y; Demura M; Nitta K; Kawano K
Biochemistry; 2002 Nov; 41(46):13807-13. PubMed ID: 12427044
[TBL] [Abstract][Full Text] [Related]
53. Is the molten globule a third thermodynamic state of protein? The example of alpha-lactalbumin.
Pfeil W
Proteins; 1998 Jan; 30(1):43-8. PubMed ID: 9443339
[TBL] [Abstract][Full Text] [Related]
54. Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates.
Engelhard M; Evans PA
Protein Sci; 1995 Aug; 4(8):1553-62. PubMed ID: 8520481
[TBL] [Abstract][Full Text] [Related]
55. Use of fluorescence decay times of 8-ANS-protein complexes to study the conformational transitions in proteins which unfold through the molten globule state.
Uversky VN; Winter S; Löber G
Biophys Chem; 1996 Jun; 60(3):79-88. PubMed ID: 8679928
[TBL] [Abstract][Full Text] [Related]
56. Pressure-induced unfolding of the molten globule of all-Ala alpha-lactalbumin.
Lassalle MW; Li H; Yamada H; Akasaka K; Redfield C
Protein Sci; 2003 Jan; 12(1):66-72. PubMed ID: 12493829
[TBL] [Abstract][Full Text] [Related]
57. Effect of the extra n-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli.
Chaudhuri TK; Horii K; Yoda T; Arai M; Nagata S; Terada TP; Uchiyama H; Ikura T; Tsumoto K; Kataoka H; Matsushima M; Kuwajima K; Kumagai I
J Mol Biol; 1999 Jan; 285(3):1179-94. PubMed ID: 9887272
[TBL] [Abstract][Full Text] [Related]
58. Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.
Kataoka M; Kuwajima K; Tokunaga F; Goto Y
Protein Sci; 1997 Feb; 6(2):422-30. PubMed ID: 9041645
[TBL] [Abstract][Full Text] [Related]
59. Cofactor-induced refolding: refolding of molten globule carbonic anhydrase induced by Zn(II) and Co(II).
Andersson D; Hammarström P; Carlsson U
Biochemistry; 2001 Mar; 40(9):2653-61. PubMed ID: 11258876
[TBL] [Abstract][Full Text] [Related]
60. Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach.
Kelkar DA; Chaudhuri A; Haldar S; Chattopadhyay A
Eur Biophys J; 2010 Sep; 39(10):1453-63. PubMed ID: 20372885
[TBL] [Abstract][Full Text] [Related]
[Previous] [Next] [New Search]