168 related articles for article (PubMed ID: 1453446)
1. Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry.
Yutani K; Ogasahara K; Kuwajima K
J Mol Biol; 1992 Nov; 228(2):347-50. PubMed ID: 1453446
[TBL] [Abstract][Full Text] [Related]
2. Molten globule of bovine alpha-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: a comparative analysis by circular dichroism spectroscopy and limited proteolysis.
Polverino de Laureto P; Frare E; Gottardo R; Fontana A
Proteins; 2002 Nov; 49(3):385-97. PubMed ID: 12360528
[TBL] [Abstract][Full Text] [Related]
3. Calorimetric determination of the energetics of the molten globule intermediate in protein folding: apo-alpha-lactalbumin.
Xie D; Bhakuni V; Freire E
Biochemistry; 1991 Nov; 30(44):10673-8. PubMed ID: 1931986
[TBL] [Abstract][Full Text] [Related]
4. Energetic basis of structural stability in the molten globule state: alpha-lactalbumin.
Griko YV
J Mol Biol; 2000 Apr; 297(5):1259-68. PubMed ID: 10764588
[TBL] [Abstract][Full Text] [Related]
5. 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]
6. Thermodynamic stability of the molten globule states of apomyoglobin.
Nishii I; Kataoka M; Goto Y
J Mol Biol; 1995 Jul; 250(2):223-38. PubMed ID: 7608972
[TBL] [Abstract][Full Text] [Related]
7. 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]
8. Cooperative thermal transitions of bovine and human apo-alpha-lactalbumins: evidence for a new intermediate state.
Veprintsev DB; Permyakov SE; Permyakov EA; Rogov VV; Cawthern KM; Berliner LJ
FEBS Lett; 1997 Aug; 412(3):625-8. PubMed ID: 9276479
[TBL] [Abstract][Full Text] [Related]
9. The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state.
Okazaki A; Ikura T; Nikaido K; Kuwajima K
Nat Struct Biol; 1994 Jul; 1(7):439-46. PubMed ID: 7664062
[TBL] [Abstract][Full Text] [Related]
10. Cold denaturation of alpha-lactalbumin.
Mizuguchi M; Hashimoto D; Sakurai M; Nitta K
Proteins; 2000 Mar; 38(4):407-13. PubMed ID: 10707027
[TBL] [Abstract][Full Text] [Related]
11. Local and long-range interactions in the molten globule state: A study of chimeric proteins of bovine and human alpha-lactalbumin.
Mizuguchi M; Masaki K; Demura M; Nitta K
J Mol Biol; 2000 May; 298(5):985-95. PubMed ID: 10801363
[TBL] [Abstract][Full Text] [Related]
12. Are the molten globule and the unfolded states of apo-alpha-lactalbumin enthalpically equivalent?
Xie D; Bhakuni V; Freire E
J Mol Biol; 1993 Jul; 232(1):5-8. PubMed ID: 8331670
[TBL] [Abstract][Full Text] [Related]
13. The chaperone-like alpha-crystallin forms a complex only with the aggregation-prone molten globule state of alpha-lactalbumin.
Rajaraman K; Raman B; Ramakrishna T; Rao CM
Biochem Biophys Res Commun; 1998 Aug; 249(3):917-21. PubMed ID: 9731236
[TBL] [Abstract][Full Text] [Related]
14. Energetics of the alpha-lactalbumin states: a calorimetric and statistical thermodynamic study.
Griko YV; Freire E; Privalov PL
Biochemistry; 1994 Feb; 33(7):1889-99. PubMed ID: 8110793
[TBL] [Abstract][Full Text] [Related]
15. Stepwise proteolytic removal of the beta subdomain in alpha-lactalbumin. The protein remains folded and can form the molten globule in acid solution.
Polverino de Laureto P; Vinante D; Scaramella E; Frare E; Fontana A
Eur J Biochem; 2001 Aug; 268(15):4324-33. PubMed ID: 11488928
[TBL] [Abstract][Full Text] [Related]
16. Vibrational Raman optical activity of alpha-lactalbumin: comparison with lysozyme, and evidence for native tertiary folds in molten globule states.
Wilson G; Ford SJ; Cooper A; Hecht L; Wen ZQ; Barron LD
J Mol Biol; 1995 Dec; 254(4):747-60. PubMed ID: 7500347
[TBL] [Abstract][Full Text] [Related]
17. pH-dependent stability of the human alpha-lactalbumin molten globule state: contrasting roles of the 6 - 120 disulfide and the beta-subdomain at low and neutral pH.
Horng JC; Demarest SJ; Raleigh DP
Proteins; 2003 Aug; 52(2):193-202. PubMed ID: 12833543
[TBL] [Abstract][Full Text] [Related]
18. Membrane-protein interaction and the molten globule state: interaction of alpha-lactalbumin with membranes.
Lala AK; Kaul P; Ratnam PB
J Protein Chem; 1995 Oct; 14(7):601-9. PubMed ID: 8561856
[TBL] [Abstract][Full Text] [Related]
19. The molten globule state of alpha-lactalbumin.
Kuwajima K
FASEB J; 1996 Jan; 10(1):102-9. PubMed ID: 8566530
[TBL] [Abstract][Full Text] [Related]
20. Hydrogen exchange study of canine milk lysozyme: stabilization mechanism of the molten globule.
Kobashigawa Y; Demura M; Koshiba T; Kumaki Y; Kuwajima K; Nitta K
Proteins; 2000 Sep; 40(4):579-89. PubMed ID: 10899783
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]