The orf63 gene resides in a region of the lambda bacteriophage genome between the exo and xis genes and is among the earliest genes transcribed during infection. In lambda phage and Shiga toxin (Stx) producing phages found in enterohemorrhagic Escherichia coli (EHEC) associated with food poisoning, Orf63 expression reduces the host survival and hastens the period between infection and lysis thereby giving it pro-lytic qualities. The NMR structure of dimeric Orf63 reveals a fold consisting of two...
[NMR paper] An NMR and MD study of complexes of bacteriophage lambda lysozyme with tetra- and hexa-N-acetylchitohexaose.
An NMR and MD study of complexes of bacteriophage lambda lysozyme with tetra- and hexa-N-acetylchitohexaose.
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Proteins. 2020 01;88(1):82-93
Authors: Turupcu A, Bowen AM, Di...
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[NMR paper] The Dynamics of Lysozyme from Bacteriophage Lambda in Solution Probed by NMR and MD Simulations.
The Dynamics of Lysozyme from Bacteriophage Lambda in Solution Probed by NMR and MD Simulations.
The Dynamics of Lysozyme from Bacteriophage Lambda in Solution Probed by NMR and MD Simulations.
Chembiochem. 2013 Jun 25;
Authors: Smith LJ, Bowen AM, Di Paolo A, Matagne A, Redfield C
Abstract
(15) N NMR relaxation studies, analyses of NMR data to include chemical shifts, residual dipolar couplings (RDC), NOEs and H(N) -H(?) coupling constants, and molecular dynamics (MD) simulations have been used to characterise the behaviour of...
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[NMR paper] Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Related Articles Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Biochemistry. 2005 Aug 2;44(30):10153-63
Authors: Mishima M, Shida T, Yabuki K, Kato K, Sekiguchi J, Kojima C
Bacillus subtilis CwlC is a cell wall lytic N-acetylmuramoyl-l-alanine amidase that plays an...
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[NMR paper] NMR assignment of the gpU tail protein from lambda bacteriophage.
NMR assignment of the gpU tail protein from lambda bacteriophage.
Related Articles NMR assignment of the gpU tail protein from lambda bacteriophage.
J Biomol NMR. 2005 May;32(1):91-2
Authors: Edmonds L, Thirumoorthy R, Liu A, Davidson A, Donaldson L
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[NMR paper] NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabi
NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabilizing protein gpD.
Related Articles NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabilizing protein gpD.
J Biomol NMR. 2005 Apr;31(4):351-6
Authors: Iwai H, Forrer P, Plückthun A, Güntert P
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[NMR paper] Structure of the coat protein in fd filamentous bacteriophage particles determined by
Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.
Related Articles Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.
Proc Natl Acad Sci U S A. 2003 May 27;100(11):6458-63
Authors: Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ
The atomic resolution structure of fd coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles differs from that previously determined...
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[NMR paper] NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of
NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif.
Related Articles NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif.
Cell. 1998 Apr 17;93(2):289-99
Authors: Legault P, Li J, Mogridge J, Kay LE, Greenblatt J
The structure of the complex formed by the arginine-rich motif of the transcriptional antitermination protein N of phage lambda and boxB RNA was determined by heteronuclear magnetic resonance...
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[NMR paper] Structure and stability of monomeric lambda repressor: NMR evidence for two-state fol
Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding.
Related Articles Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding.
Biochemistry. 1995 Mar 28;34(12):3884-92
Authors: Huang GS, Oas TG
The absence of equilibrium intermediates in protein folding reactions (i.e., two-state folding) simplifies thermodynamic and kinetic analyses but is difficult to prove rigorously. We demonstrate a sensitive method for detecting partially folded species based on using proton chemical...