94 related articles for article (PubMed ID: 9410027)
1. [NMR study of beta-structures in the compact non-native states of globular proteins].
Kutyshenko AV; Kutyshenko VP; Kivaeva LS
Biofizika; 1997; 42(5):1015-9. PubMed ID: 9410027
[TBL] [Abstract][Full Text] [Related]
2. Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins.
Redfield C
Methods; 2004 Sep; 34(1):121-32. PubMed ID: 15283921
[TBL] [Abstract][Full Text] [Related]
3. Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study.
Kutyshenko VP; Cortijo M
Protein Sci; 2000 Aug; 9(8):1540-7. PubMed ID: 10975575
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. [Spin diffusion in globular proteins: alpha-lactalbumin].
Kutyshenko VP; Prokhorov DA; Khristoforov VS
Biofizika; 2004; 49(4):601-7. PubMed ID: 15458242
[TBL] [Abstract][Full Text] [Related]
6. Compact intermediates states in protein folding.
Fink AL
Subcell Biochem; 1995; 24():27-53. PubMed ID: 7900179
[No Abstract] [Full Text] [Related]
7. Transient non-native secondary structures during the refolding of alpha-lactalbumin detected by infrared spectroscopy.
Troullier A; Reinstädler D; Dupont Y; Naumann D; Forge V
Nat Struct Biol; 2000 Jan; 7(1):78-86. PubMed ID: 10625432
[TBL] [Abstract][Full Text] [Related]
8. Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy.
Schanda P; Forge V; Brutscher B
Proc Natl Acad Sci U S A; 2007 Jul; 104(27):11257-62. PubMed ID: 17592113
[TBL] [Abstract][Full Text] [Related]
9. [Secondary structure of proteins from circular dichroism spectra. V. Secondary structure of proteins in a "molten globule" state].
Bolotina IA
Mol Biol (Mosk); 1987; 21(6):1625-35. PubMed ID: 3128730
[TBL] [Abstract][Full Text] [Related]
10. Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy.
Wijesinha-Bettoni R; Dobson CM; Redfield C
J Mol Biol; 2001 Mar; 307(3):885-98. PubMed ID: 11273708
[TBL] [Abstract][Full Text] [Related]
11. 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]
12. Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin.
Cavagnero S; Dyson HJ; Wright PE
J Mol Biol; 1999 Jan; 285(1):269-82. PubMed ID: 9878405
[TBL] [Abstract][Full Text] [Related]
13. Diffusive motions control the folding and unfolding kinetics of the apomyoglobin pH 4 molten globule intermediate.
Ramos CH; Weisbuch S; Jamin M
Biochemistry; 2007 Apr; 46(14):4379-89. PubMed ID: 17367166
[TBL] [Abstract][Full Text] [Related]
14. [Study of water-protein interaction by high resolution NMR].
Kutyshenko VP
Mol Biol (Mosk); 2001; 35(1):90-9. PubMed ID: 11234387
[TBL] [Abstract][Full Text] [Related]
15. 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; 49(1):95-103. PubMed ID: 12211019
[TBL] [Abstract][Full Text] [Related]
16. Alpha-lactalbumin forms a compact molten globule in the absence of disulfide bonds.
Redfield C; Schulman BA; Milhollen MA; Kim PS; Dobson CM
Nat Struct Biol; 1999 Oct; 6(10):948-52. PubMed ID: 10504730
[TBL] [Abstract][Full Text] [Related]
17. The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study.
Carver JA; Lindner RA; Lyon C; Canet D; Hernandez H; Dobson CM; Redfield C
J Mol Biol; 2002 May; 318(3):815-27. PubMed ID: 12054825
[TBL] [Abstract][Full Text] [Related]
18. Conformational flexibility of alpha-lactalbumin related to its membrane binding capacity.
Halskau O; Underhaug J; Frøystein NA; Martínez A
J Mol Biol; 2005 Jun; 349(5):1072-86. PubMed ID: 15913646
[TBL] [Abstract][Full Text] [Related]
19. 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]
20. Local unfolding is required for the site-specific protein modification by transglutaminase.
Spolaore B; Raboni S; Ramos Molina A; Satwekar A; Damiano N; Fontana A
Biochemistry; 2012 Oct; 51(43):8679-89. PubMed ID: 23083324
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]