Related ArticlesNMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.
J Biol Chem. 2004 Aug 13;279(33):34963-70
Authors: Santiveri CM, Pérez-Cañadillas JM, Vadivelu MK, Allen MD, Rutherford TJ, Watkins NA, Bycroft M
The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free alpha-hemoglobin, has been determined using NMR spectroscopy. The protein native state shows conformational heterogeneity attributable to the isomerization of the peptide bond preceding a conserved proline residue. The two equally populated cis and trans forms both adopt an elongated antiparallel three alpha-helix bundle fold but display major differences in the loop between the first two helices and at the C terminus of helix 3. Proline to alanine single point mutation of the residue Pro-30 prevents the cis/trans isomerization. The structure of the P30A mutant is similar to the structure of the trans form of AHSP in the loop 1 region. Both the wild-type AHSP and the P30A mutant bind to alpha-hemoglobin, and the wild-type conformational heterogeneity is quenched upon complex formation, suggesting that just one conformation is the active form. Changes in chemical shift observed upon complex formation identify a binding interface comprising the C terminus of helix 1, the loop 1, and the N terminus of helix 2, with the exposed residues Phe-47 and Tyr-51 being attractive targets for molecular recognition. The characteristics of this interface suggest that AHSP binds at the intradimer alpha1beta1 interface in tetrameric HbA.
[NMR paper] Insights into conformation and dynamics of protein GB1 during folding and unfolding b
Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR.
Related Articles Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR.
J Mol Biol. 2004 Jan 30;335(5):1299-307
Authors: Ding K, Louis JM, Gronenborn AM
Understanding protein stability requires characterization of structural determinants of the folded and unfolded states. Many proteins are capable of populating partially folded states under specific solution conditions. Occasionally, coexistence of the folded and an...
nmrlearner
Journal club
0
11-24-2010 09:25 PM
[NMR paper] The membrane-bound conformation of alpha-lactalbumin studied by NMR-monitored 1H exch
The membrane-bound conformation of alpha-lactalbumin studied by NMR-monitored 1H exchange.
Related Articles The membrane-bound conformation of alpha-lactalbumin studied by NMR-monitored 1H exchange.
J Mol Biol. 2002 Aug 2;321(1):99-110
Authors: Halskau Ø, Frøystein NA, Muga A, Martínez A
The interaction of bovine alpha-lactalbumin (BLA) with negatively charged phospholipid bilayers was studied by NMR monitored 1H exchange to characterize the conformational transition that enables a water-soluble protein to associate with and partially insert...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] Helix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and T
Helix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and TFE solutions: 2D-1H NMR and CD studies in alanine-lysine peptides.
Related Articles Helix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and TFE solutions: 2D-1H NMR and CD studies in alanine-lysine peptides.
Biochemistry. 1998 Dec 8;37(49):17318-30
Authors: Padmanabhan S, Jiménez MA, Laurents DV, Rico M
Interactions between side chains spaced (i,i + 3) and (i,i + 4) may explain the context dependence of helix propensities observed...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through
Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
Related Articles Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
J Biol Chem. 1998 Oct 16;273(42):27357-63
Authors: McInnes C, Wang J, Al Moustafa AE, Yansouni C, O'Connor-McCourt M, Sykes BD
The investigation of a...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Insights into the mechanism of heterodimerization from the 1H-NMR solution structure
Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
Related Articles Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
J Mol Biol. 1998 Aug 7;281(1):165-81
Authors: Lavigne P, Crump MP, Gagné SM, Hodges RS, Kay CM, Sykes BD
The oncoprotein c-Myc (a member of the helix-loop-helix-leucine zipper (b-HLH-LZ) family of transcription factors) must heterodimerize with the b-HLH-LZ Max...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and c
NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Related Articles NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Int J Biol Macromol. 1998 May-Jun;22(3-4):197-209
Authors: Carver JA, Lindner RA
The subunit molecular mass of alpha-crystallin, like many small heat-shock proteins (sHsps), is around 20 kDa although the protein exists as a large aggregate of average mass around 800...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
[NMR paper] NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
Related Articles NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
Basic Life Sci. 1990;56:231-53
Authors: Berliner LJ, Kaptein R, Koga K, Musci G