Related ArticlesStructure and dynamics of the M13 coat signal sequence in membranes by multidimensional high-resolution and solid-state NMR spectroscopy.
Proteins. 1997 Apr;27(4):481-92
Authors: Bechinger B
The polypeptide corresponding to the signal sequence of the M13 coat protein and the five N-terminal residues of the mature protein was prepared by solid-phase peptide synthesis with a 15N isotopic label at the alanine-12 position. Multidimensional solution NMR spectroscopy and molecular modeling calculations indicate that this polypeptide assumes helical conformations between residues 5 and 20, in the presence of sodium dodecylsulfate micelles. This is in good agreement with circular dichroism spectroscopic measurement, which shows an alpha-helix content of approximately 42%. The alpha-helix comprises an uninterrupted hydrophobic stretch of < or = 12 amino acids, which is generally believed to be too short for a stable transmembrane alignment in a biological bilayer. The monoexponential proton-deuterium exchange kinetics of this hydrophobic helical region is characterized by half-lives of 15-75 minutes (pH 4.2, 323 K). When the polypeptide is reconstituted into phospholipid bilayers, the broad anisotropy of the proton-decoupled 15N solid-state NMR spectroscopy indicates that the hydrophobic helix is immobilized close to the lipid bilayer surface at the time scale of 15N solid-state NMR spectroscopy (10(-4) seconds). By contrast, short correlation times, immediate hydrogen-deuterium exchange as well as nuclear Overhauser effect crosspeak analysis suggest that the N and C termini of this polypeptide exhibit a mobile random coil structure. The implications of these structural findings for possible mechanisms of membrane insertion and translocation as well as for membrane protein structure prediction algorithms are discussed.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
J Struct Funct Genomics. 2011 Sep 9;
Authors: Yang Y, Ramelot TA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA
Abstract
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[NMR paper] Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spec
Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.
Related Articles Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.
J Mol Biol. 2004 Aug 13;341(3):869-79
Authors: Thiriot DS, Nevzorov AA, Zagyanskiy L, Wu CH, Opella SJ
The atomic resolution structure of Pf1 coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles in solution is compared to the structures previously determined by X-ray fiber and...
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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] Structure and dynamics of the M13 coat signal sequence in membranes by multidimension
Structure and dynamics of the M13 coat signal sequence in membranes by multidimensional high-resolution and solid-state NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Structure and dynamics of the M13 coat signal sequence in membranes by multidimensional high-resolution and solid-state NMR spectroscopy.
Proteins. 1997 Apr;27(4):481-92
Authors: Bechinger B
The polypeptide corresponding to the signal sequence of the...
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[NMR paper] Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by sol
Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR.
Biochemistry. 1996 Apr 23;35(16):5145-57
Authors: Williams KA, Farrow NA, Deber CM, Kay LE
The structure and dynamics of the 53-residue filamentous bacteriophage IKe major coat protein in fully protonated myristoyllysophosphatidylglycerol (MPG)...
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[NMR paper] NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat pr
NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
Related Articles NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
Science. 1991 May 31;252(5010):1303-5
Authors: Shon KJ, Kim Y, Colnago LA, Opella SJ
Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles....
Structure and dynamics of the M13 coat signal sequence in membranes by multidimension
Linear Mode
