@article {1484,
	title = {Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane},
	journal = {Journal of Molecular Biology},
	volume = {355},
	number = {2},
	year = {2006},
	note = {ISI Document Delivery No.: 999EPTimes Cited: 30Cited Reference Count: 84},
	month = {Jan},
	pages = {294-309},
	type = {Article},
	abstract = {Filamentous bacteriophage (Inovirus) is a simple and well-characterized model system. The phage particle, or virion, is about 60 A in diameter and several thousand angstrom units long. The virions are assembled at the bacterial membrane as they extrude out of the host without killing it, an example of specific transport of nucleoprotein assemblages across membranes. The Ff group (fd, f1. and M13) has been especially widely studied. Models of virion assembly have been proposed based on a molecular model of the fd virion derived by X-ray fibre diffraction. A somewhat different model of the fd virion using solid-state NMR data has been proposed, not consistent with these models of assembly nor with the X-ray diffraction data. Here we show that reinterpreted NMR data are also consistent with the model derived from X-ray fibre diffraction studies, and discuss models of virion assembly. (c) 2005 Elsevier Ltd. All rights reserved.},
	keywords = {ALPHA-HELICES, ALPHA-HELIX, ATOMIC REFINEMENT, fibre diffraction, filamentous bacteriophage, INOVIRUS, MAJOR COAT PROTEIN, MEMBRANE, ORIENTATIONAL RESTRAINTS, PF1 BACTERIOPHAGE, PISEMA, PROTEINS, RESOLUTION, SINGLE-STRANDED-DNA, VIRION, VIRUS},
	isbn = {0022-2836},
	url = {<Go to ISI>://000234371900012},
	author = {Marvin, D. A. and Welsh, L. C. and Symmons, M. F. and Scott, W. R. P. and Straus, S. K.}
}
@article {1291,
	title = {Plasticity of influenza haemagglutinin fusion peptides and their interaction with lipid bilayers},
	journal = {Biophysical Journal},
	volume = {88},
	number = {1},
	year = {2005},
	note = {ISI Document Delivery No.: 884MYTimes Cited: 36Cited Reference Count: 72},
	month = {Jan},
	pages = {25-36},
	type = {Article},
	abstract = {A detailed molecular dynamics study of the haemagglutinin fusion peptide (N-terminal 20 residues of the HA2 subunits) in a model bilayer has yielded useful information about the molecular interactions leading to insertion into the lipids. Simulations were performed on the native sequence, as well as a number of mutant sequences, which are either fusogenic or nonfusogenic. For the native sequence and fusogenic mutants, the N-terminal 11 residues of the fusion peptides are helical and insert with a tilt angle of similar to30degrees with respect to the membrane normal, in very good agreement with experimental data. The tilted insertion of the native sequence peptide leads to membrane bilayer thinning and the calculated order parameters show larger disorder of the alkyl chains. These results indicate that the lipid packing is perturbed by the fusion peptide and could be used to explain membrane fusion. For the nonfusogenic sequences investigated, it was found that most of them equilibrate parallel to the interface plane and do not adopt a tilted conformation. The presence of a charged residue at the beginning of the sequence (G1E mutant) resulted in a more difficult case, and the outcomes do not fall straightforwardly into the general picture. Sequence searches have revealed similarities of the fusion peptide of influenza haemagglutinin with peptide sequences such as segments of porin, amyloid ab peptide, and a peptide from the prion sequence. These results confirm that the sequence can adopt different folds in different environments. The plasticity and the conformational dependence on the local environment could be used to better understand the function of fusion peptides.},
	keywords = {ANALOGS, CONFORMATION, HEMAGGLUTININ, MEDIATED MEMBRANE-FUSION, MODEL MEMBRANES, MOLECULAR-DYNAMICS SIMULATION, MULTIPLE ALIGNMENT, RECEPTOR-BINDING, SEQUENCE, VIRAL FUSION, VIRUS},
	isbn = {0006-3495},
	url = {<Go to ISI>://000226090900006},
	author = {Vaccaro, L. and Cross, K. J. and Kleinjung, J. and Straus, S. K. and Thomas, D. J. and Wharton, S. A. and Skehel, J. J. and Fraternali, F.}
}
