Related Articlesalpha-->beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR.
J Mol Biol. 1998 Nov 6;283(4):731-9
Authors: Kuwata K, Hoshino M, Era S, Batt CA, Goto Y
Whereas bovine beta-lactoglobulin is a predominantly beta-sheet protein, it has a marked alpha-helical preference and can be considered to be a useful model of the alpha-->beta transition, a key issue for understanding the folding and biological function of a number of proteins. In order to understand the mechanism of the alpha-->beta transition, the backbone structures of the recombinant bovine beta-lactoglobulin A in the native state and in the highly helical state induced by 2,2,2-trifluoroethanol were characterized by 1H, 13C and 15N multidimensional NMR spectroscopy. Overall, the secondary structures in the native state were similar to those of the crystal structure. On the other hand, beta-lactoglobulin in the 2,2,2-trifluoroethanol state was composed of many alpha-helical segments. The presence of the persistent alpha-helices in the helical state and the core beta-sheet in the native state suggested that during folding native-like core beta-sheet and several non-native helices are formed first and the remaining beta-sheet is subsequently "induced" through interaction with the pre-existing beta-sheet.
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation [Biochemistry]
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation
Metcalf, D. G., Moore, D. T., Wu, Y., Kielec, J. M., Molnar, K., Valentine, K. G., Wand, A. J., Bennett, J. S., DeGrado, W. F....
Date: 2010-12-28
The integrin IIbβ3 is a transmembrane (TM) heterodimeric adhesion receptor that exists in equilibrium between resting and active ligand binding conformations. In resting IIbβ3, the TM and cytoplasmic domains of IIb and β3 form a heterodimer that constrains IIbβ3 in its resting conformation. To study the structure...
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NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation.
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation.
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation.
Proc Natl Acad Sci U S A. 2010 Dec 14;
Authors: Metcalf DG, Moore DT, Wu Y, Kielec JM, Molnar K, Valentine KG, Wand AJ, Bennett JS, Degrado WF
The integrin ?IIb?3 is a transmembrane (TM) heterodimeric adhesion receptor that exists in equilibrium between resting and active ligand binding conformations. In resting ?IIb?3, the TM and...
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[NMR paper] Assignment of 1H(N), 15N, 13C(alpha), 13CO and 13C(beta) resonances in a 67 kDa p53 d
Assignment of 1H(N), 15N, 13C(alpha), 13CO and 13C(beta) resonances in a 67 kDa p53 dimer using 4D-TROSY NMR spectroscopy.
Related Articles Assignment of 1H(N), 15N, 13C(alpha), 13CO and 13C(beta) resonances in a 67 kDa p53 dimer using 4D-TROSY NMR spectroscopy.
J Biomol NMR. 2000 Oct;18(2):173-6
Authors: Mulder FA, Ayed A, Yang D, Arrowsmith CH, Kay LE
The p53 tumor suppressor is a transcription factor that plays a crucial role in the activation of genes in response to DNA damage. As a first step towards detailed structural studies of the...
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[NMR paper] Isotopically labeled bovine beta-lactoglobulin for NMR studies expressed in Pichia pa
Isotopically labeled bovine beta-lactoglobulin for NMR studies expressed in Pichia pastoris.
Related Articles Isotopically labeled bovine beta-lactoglobulin for NMR studies expressed in Pichia pastoris.
Protein Expr Purif. 1998 Oct;14(1):97-103
Authors: Denton H, Smith M, Husi H, Uhrin D, Barlow PN, Batt CA, Sawyer L
beta-Lactoglobulin (beta-Lg) is the major whey protein in ruminant milk and has been implicated in the irreversible denaturation of milk proteins and its associated poor processing behavior during heat treatment. In order to help...
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[NMR paper] High helicity of peptide fragments corresponding to beta-strand regions of beta-lacto
High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
Related Articles High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
Fold Des. 1996;1(4):255-63
Authors: Kuroda Y, Hamada D, Tanaka T, Goto Y
BACKGROUND: Whereas protein fragments, when they are structured, adopt conformations similar to that found in the native state, the high helical propensity of beta-lactoglobulin, a predominantly beta-sheet...
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[NMR paper] Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
Biochemistry. 1996 Sep 10;35(36):11577-88
Authors: Drohat AC, Amburgey JC, Abildgaard F, Starich MR, Baldisseri D, Weber DJ
S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with noncovalent interactions at its dimer interface. Each apo-S100 beta...
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[NMR paper] High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensio
High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Related Articles High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Science. 1994 Mar 25;263(5154):1762-7
Authors: Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM
The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional...
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[NMR paper] High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensio
High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Related Articles High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Science. 1994 Mar 25;263(5154):1762-7
Authors: Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM
The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional...