@article {2148,
	title = {{\textquoteright}Mechanical Engineering{\textquoteright} of Elastomeric Proteins: Toward Designing New Protein Building Blocks for Biomaterials},
	journal = {Advanced Functional Materials},
	volume = {18},
	number = {18},
	year = {2008},
	note = {ISI Document Delivery No.: 358QQTimes Cited: 6Cited Reference Count: 102Li, Hongbin},
	month = {Sep},
	pages = {2643-2657},
	type = {Review},
	abstract = {Elastomeric proteins are subject to stretching force under biological settings and play important roles in regulating the mechanical properties of a wide range of biological machinery. Elastomeric proteins also underlie the superb mechanical properties of many protein-based biomaterials. The developments of single molecule force spectroscopy have enabled the direct characterization of the mechanical properties of elastomeric proteins at the single molecule level and led to the new burgeoning field of research: single protein mechanics-and engineering. Combined, single molecule atomic force microscopy and protein engineering efforts are well under way to understand molecular determinants for the mechanical stability of elastomeric proteins and to develop methodologies to tune the mechanical properties of proteins in a rational and systematic fashion, which will lead to the {\textquoteright}mechanical engineering{\textquoteright} of elastomeric proteins. Here the current status of these experimental efforts is discussed and the successes and challenges in constructing novel proteins with tailored nanomechanical proteins are highlighted. The prospect of employing such engineered artificial elastomeric proteins as building blocks for the construction of biomaterials for applications ranging from material sciences to biomedical engineering is also discussed.},
	keywords = {ATOMIC-FORCE MICROSCOPY, BIOLOGICAL ROLES, DIHYDROFOLATE-REDUCTASE, EXTRACELLULAR-MATRIX PROTEIN, FLUORESCENT PROTEIN, IG DOMAIN, MOLECULAR-DYNAMICS SIMULATIONS, PROTEIN, SINGLE, TITIN IMMUNOGLOBULIN DOMAINS, UNFOLDING PATHWAYS},
	isbn = {1616-301X},
	url = {<Go to ISI>://000259933000001},
	author = {Li, H. B.}
}
@article {1555,
	title = {Engineering proteins with novel mechanical properties by recombination of protein fragments},
	journal = {Angewandte Chemie-International Edition},
	volume = {45},
	number = {34},
	year = {2006},
	note = {ISI Document Delivery No.: 082MRTimes Cited: 20Cited Reference Count: 51Sharma, Deepak Cao, Yi Li, Hongbin},
	pages = {5633-5638},
	type = {Article},
	keywords = {AFM, ATOMIC-FORCE MICROSCOPY, ELASTICITY, EVOLUTION, IG DOMAIN, IMMUNOGLOBULIN DOMAINS, MOLECULAR-DYNAMICS SIMULATIONS, protein engineering, protein structures, scanning probe microscopy, SINGLE PROTEIN, single-molecule studies, SPECTROSCOPY, STABILITY, TITIN},
	isbn = {1433-7851},
	url = {<Go to ISI>://000240391400016},
	author = {Sharma, D. and Cao, Y. and Li, H. B.}
}
@article {1371,
	title = {Structures and rearrangements of LiCl clusters},
	journal = {Journal of Chemical Physics},
	volume = {124},
	number = {24},
	year = {2006},
	note = {ISI Document Delivery No.: 059KBTimes Cited: 3Cited Reference Count: 15},
	month = {Jun},
	pages = {7},
	type = {Article},
	abstract = {Molecular dynamics simulations are used to investigate the low-temperature structures and temperature-driven rearrangements of (LiCl)(n) clusters, with n ranging from 3 to 500. It is found that for n <= 32 expanded, ring-based structures are energetically more stable than cubic (rocksalt) forms at low temperature. For n >= 108, the cubic structures are lower in energy, but as the clusters are heated rearrangements to expanded structures occur well below the melting temperature. Hexagonal (LiCl)(3) rings are a distinguishing feature of the expanded, ring-based structures. Highly asymmetric ion sizes are essential for the formation of the expanded structures. Similar transitions from more-ordered to less-ordered solid states are not found for corresponding (KCl)(n) clusters, which remain in the cubic structure until they melt. (c) 2006 American Institute of Physics.},
	keywords = {ALKALI-HALIDES, MOLECULAR-DYNAMICS SIMULATIONS},
	isbn = {0021-9606},
	url = {<Go to ISI>://000238730600028},
	author = {Croteau, T. and Patey, G. N.}
}
@article {1063,
	title = {Can PISEMA experiments be used to extract structural parameters for mobile beta-barrels?},
	journal = {Journal of Biomolecular Nmr},
	volume = {32},
	number = {2},
	year = {2005},
	note = {ISI Document Delivery No.: 948CRTimes Cited: 4Cited Reference Count: 42},
	month = {Jun},
	pages = {101-111},
	type = {Article},
	abstract = {The effect of mobility on N-15 chemical shift/N-15-H-1 dipolar coupling (PISEMA) solid state NMR experiments applied to macroscopically oriented beta-barrels is assessed using molecular dynamics simulation data of the NalP autotransporter domain embedded in a DMPC bilayer. In agreement with previous findings for alpha-helices, the fast librational motion of the peptide planes is found to have a considerable effect on the calculated PISEMA spectra. In addition, the dependence of the chemical shift anisotropy (CSA) and dipolar coupling parameters on the calculated spectra is evaluated specifically for the beta-barrel case. It is found that the precise choice of the value of the CSA parameters sigma(11), sigma(22) and sigma(33) has only a minor effect, whereas the choice of the CSA parameter theta shifts the position of the peaks by up to 20 ppm and changes the overall shape of the spectrum significantly. As was found for alpha-helices, the choice of the NH bond distance has a large effect on the dipolar coupling constant used for the calculations. Overall, it is found that the alternating beta-strands in the barrel occupy distinct regions of the PISEMA spectra, forming patterns which may prove useful in peak assignment.},
	keywords = {ANGLE-SPINNING NMR, ASSIGNMENT, COAT PROTEIN, CONSTRAINTS, DOMAIN, HELICAL WHEELS, MEMBRANE-PROTEINS, mobility of membrane beta-barrels, MOLECULAR-DYNAMICS SIMULATIONS, mosaic spread, PISEMA, SOLID-STATE NMR, SPECTROSCOPY, time averaging},
	isbn = {0925-2738},
	url = {<Go to ISI>://000230694100001},
	author = {Bleile, D. W. and Scott, W. R. P. and Straus, S. K.}
}
@article {1093,
	title = {Interaction of alamethicin with ether-linked phospholipid bilayers: Oriented circular dichroism, P-31 solid-state NMR, and differential scanning calorimetry studies},
	journal = {Biophysical Journal},
	volume = {89},
	number = {4},
	year = {2005},
	note = {ISI Document Delivery No.: 968FPTimes Cited: 22Cited Reference Count: 60},
	month = {Oct},
	pages = {2434-2442},
	type = {Article},
	abstract = {The arrangement of the antimicrobial peptide alamethicin was studied by oriented circular dichroism, 31 P solidstate NMR, and differential scanning calorimetry in ether- linked phospholipid bilayers composed of 1,2-O-dihexadecyl- sn-glycero3- phosphocholine ( DHPC). The measurements were performed as a function of alamethicin concentration relative to the lipid concentration, and results were compared to those reported in the literature for ester-linked phospholipid bilayers. At ambient temperature, alamethicin incorporates into the hydrophobic core of DHPC bilayers but results in more lipid disorder than observed for ester-linked 1-palmitoyl, 2-oleoyl-sn-glycero-3-phosphatidylcholine ( POPC) lipid bilayers. This orientational disorder appears to depend on lipid properties such as bilayer thickness. Moreover, the results suggest that alamethicin inserts into the hydrophobic core of the bilayers ( at high peptide concentration) for both ether- and ester-linked lipids but using a different mechanism, namely toroidal for DHPC and barrel-stave for POPC.},
	keywords = {BIOLOGICAL-MEMBRANES, CYTOCHROME-C, DIPHYTANOYL PHOSPHATIDYLCHOLINE, FUSION PEPTIDES, HYDROPHOBIC MISMATCH, LIPID-BILAYER, MOLECULAR-DYNAMICS SIMULATIONS, NUCLEAR-MAGNETIC-RESONANCE, THERMOTROPIC PHASE-BEHAVIOR, X-RAY-DIFFRACTION},
	isbn = {0006-3495},
	url = {<Go to ISI>://000232147600025},
	author = {Dave, P. C. and Billington, E. and Pan, Y. L. and Straus, S. K.}
}
@article {4365,
	title = {Conformation of native, reduced and [5-55](Ala) bovine pancreatic trypsin inhibitor in the gas phase},
	journal = {Rapid Communications in Mass Spectrometry},
	volume = {12},
	number = {1},
	year = {1998},
	note = {ISI Document Delivery No.: YQ873Times Cited: 14Cited Reference Count: 46},
	pages = {40-44},
	type = {Article},
	abstract = {Collision cross sections have been measured for gas phase ions of native oxidized bovine pancreatic trypsin inhibitor (BPTI), native reduced BPTI and a mutant form of BPTI containing a single disulphide bond between residues 5 and 55 ([5-55](Ala) BPTI). Cross sections for [5-55](Ala) BPTI and reduced BPTI were 9\% and 17\% greater respectively than those for native BPTI, Cross sections for native BPTI were smaller than previous estimates from the crystal structure but in reasonable agreement with values calculated from the radius of gyration determined by x-ray scattering from solution BPTI. The increase in cross section for reduced BPTI over native BPTI is similar to that seen in molecular dynamics simulations, The results show that the disulphide bonds of BPTI contribute to the folding of the gas phase ions, but that even in the absence of disulphide bonds the protein ions maintain compact structures. Comparisons to relative areas calculated from hydrodynamic radii of BPTI in solution suggest that when disulphide linkages are removed, BPTI in the gas phase unfolds less than BPTI in solution. (C) 1998 John Wiley \& Sons, Ltd.},
	keywords = {BPTI, DISULFIDE BOND, IONS, MASS-SPECTROMETRY, MOLECULAR-DYNAMICS SIMULATIONS, MYOGLOBIN, protein dynamics, STABILITY},
	isbn = {0951-4198},
	url = {<Go to ISI>://000071433000008},
	author = {Nesatiy, V. and Chen, Y. L. and Collings, B. A. and Douglas, D. J.}
}
