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Bioorg Med Chem Lett. 2010 Feb 1;20(3):1260-2
Authors: Lv G, Dong S
NMR spectroscopy and molecular dynamics simulations show that BAM8-22 (Val(8)-Gly(9)-Arg(10)-Pro(11)-Glu(12)-Trp(13)-Trp(14)-Met(15)-Asp(16)-Tyr(17)-Gln(18)-Lys(19)-Arg(20)-Tyr(21)-Gly(22)) possesses a relatively well-defined alpha-helix extending from Glu(12) to Arg(20), whereas both termini remain highly flexible in aqueous solution. The conformation-activity relationship of BAM8-22 indicates that the integrity of the well-defined alpha-helical structure is essential but not the sole determining factor for its bioactivity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
J Biol Chem. 2011 May 3;
Authors: Shin J, Chakraborty G, Bharatham N, Kang C, Tochio N, Koshiba S, Kigawa T, Kim W, Kim KT, Yoon HS
Vaccinia-related kinase 1 (VRK1) is one of the mitotic kinases which play important roles in cell cycle, nuclear condensation and transcription regulation. Kinase...
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[NMR paper] Structural investigation of pig metmyoglobin by 129Xe NMR spectroscopy.
Structural investigation of pig metmyoglobin by 129Xe NMR spectroscopy.
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Biochim Biophys Acta. 2004 Sep 24;1674(2):182-92
Authors: Corda M, Era B, Fais A, Casu M
The potentiality of xenon's sensitivity to its local magnetic environment is thoroughly investigated to probe internal structural differences between pig and horse metmyoglobin (MMb). These MMb's differ by 14 amino acids. One of these, Ile142 in horse MMb, is located in the proximal cavity, which...
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Structural, NMR spectroscopic, and computational investigation of hemin loading in th
Structural, NMR spectroscopic, and computational investigation of hemin loading in the hemophore HasAp from Pseudomonas aeruginosa.
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J Am Chem Soc. 2010 Jul 21;132(28):9857-72
Authors: Jepkorir G, Rodríguez JC, Rui H, Im W, Lovell S, Battaile KP, Alontaga AY, Yukl ET, Moënne-Loccoz P, Rivera M
When challenged by low-iron conditions several Gram-negative pathogens secrete a hemophore (HasA) to scavenge...
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Towards a structural understanding of the smallest known oncoprotein: Investigation o
Towards a structural understanding of the smallest known oncoprotein: Investigation of the Bovine Papillomavirus E5 protein using solution-state NMR.
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Biochim Biophys Acta. 2010 Nov 9;
Authors: King G, Oates J, Patel D, van den Berg HA, Dixon AM
The homo-dimeric E5 protein from Bovine Papillomavirus activates the platelet-derived growth factor ? receptor through transmembrane (TM)...
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[NMR paper] NMR investigation of the solution conformation of oxidized flavodoxin from Desulfovib
NMR investigation of the solution conformation of oxidized flavodoxin from Desulfovibrio vulgaris. Determination of the tertiary structure and detection of protein-bound water molecules.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR investigation of the solution conformation of oxidized flavodoxin from Desulfovibrio vulgaris. Determination of the tertiary structure and detection of protein-bound water molecules.
Eur J Biochem. 1996 Jun...
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[NMR paper] Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR s
Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy.
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J Biol Chem. 1994 Dec 30;269(52):32909-15
Authors: Kim KS, Clark-Lewis I, Sykes BD
The three-dimensional solution structure of the growth-related protein-alpha/melanoma growth stimulatory activity (GRO/MGSA) has been solved by two-dimensional 1H nuclear magnetic resonance spectroscopy. The GRO/MGSA monomer consists of an NH2-terminal...
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[NMR paper] Conformation of MeAla6-cyclosporin A by NMR. Relationship of sidechain orientation of
Conformation of MeAla6-cyclosporin A by NMR. Relationship of sidechain orientation of the MeBmt-1, MeLeu-9, and MeLeu-10 residues to immunosuppressive activity.
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Int J Pept Protein Res. 1991 May;37(5):351-63
Authors: Gooley PR, Durette PL, Boger J, Armitage IM
MeAla6-cyclosporin A (MeAla6-CsA) is a unique CsA analog that shows weak immunosuppressive activity and yet...