Author: claimsbot

1. A packaging machine comprising:
a moulding station having at least one heating surface with a plurality of heater elements per heating surface; and
a controller configured to individually control the heater elements in order to bring different regions of a film to different temperature levels;
wherein the heater elements are formed as thick-film heater elements.
2. A packaging machine according to claim 1 wherein the at least one heating surface is configured as a heating plate, a stamp andor surfaces of a moulding cavity.
3. A packaging machine according to claim 1 wherein the heater elements are integrated into a common heating plate or heating mat.
4. A packaging machine according to claim 1 wherein that at least one heating surface comprises two mutually facing heating surfaces, and wherein the heater elements arranged on one heating surface are mirrored with the heater elements on the other heating surface.
5. A packaging machine according to claim 1 wherein the at least one heating surface comprises a plurality of heating surfaces that can be heated independently of one another.
6. A packaging machine according to claim 1 wherein the moulding station is configured to perform a moulding process on the film, and wherein the at least one heating surface is coolable during the moulding process.
7. A packaging machine according to claim 1 wherein the packaging machine is implemented as a deep-draw packaging machine with an intermittent operational cycle.
8. A packaging machine according to claim 1 wherein the film is a plastic film.
9. A method for an intermittently operating a deep-draw packaging machine with a moulding station, the method comprising:
feeding a film into the moulding station, wherein the moulding station comprises at least one heating surface with a plurality of heater elements formed as thick-film heater elements, wherein the heater elements are controllable individually by a controller in order to heat the film to different temperature levels;
closing the moulding station to create a tightly closed chamber;
controlling the heater elements with the controller for a spatially inhomogeneous temperature distribution in the film;
positioning the film on the heater elements;
switching off the heater elements after reaching the different temperature levels in the film;
deforming the film in a mould tool part of the moulding station;
cooling the film in a stable and no longer plastically deformable temperature range;
opening the moulding station; and
removing the deformed film from the moulding station.
10. A method according to claim 9 wherein the at least one heating surface comprises at least two mutually facing heating surfaces on which the heater elements are in each case mirrored with respect to one another, wherein in each case two mutually facing heater elements are operated together on the oppositely situated heating surfaces.
11. A method according to 9 wherein the at least one heating surface comprises a plurality of heating surfaces, of which at a point in time only one is heated at least progressively.

The claims below are in addition to those above.
All refrences to claim(s) which appear below refer to the numbering after this setence.

1. A method of mapping the strain in a crystalline sample, comprising:
scanning in at least one direction to form a high angle annular dark field scanning transmission electron microscope (HAADF-STEM) image of said crystalline sample including at least two regions with different strain where a Fourier transform defractogram of said HAADF-STEM image includes (111) Bragg reflections;
selecting two independent Bragg reflections in said Fourier transform defractogram;
performing geometric phase analysis (GPA) with said two said independent Bragg reflections; and
forming a strain map of said sample for at least one term in a two dimensional strain tensor.
2. The method of claim 1 where said sample has an area between about 50 nm by 50 nm and about 300 nm by 300 nm and a thickness between about 50 nm and about 250 nm.
3. The method of claim 1 where said sample has an area of about 250 nm by 250 nm and a thickness of about 200 nm.
4. The method of claim 1 where said sample is a semiconductor device and where said HAADF-STEM image includes more than one portion of said semiconductor device.
5. The method of claim 4 where said sample is a MOS transistor and said HAADF-STEM image includes at least a portion of a source, drain, channel, and substrate of said MOS transistor.
6. The method of claim 4 where said sample is a bipolar transistor and said HAADF-STEM image includes at least a portion of an emitter, a base, a collector, and a substrate of said bipolar transistor.
7. The method of claim 1 where strain maps for horizontal strain related terms, \u2208xx and \u2208x, in said two dimensional strain tensor are formed from HAADF-STEM images formed by scanning in a horizontal, x-direction and said strain maps for vertical strain related terms, \u2208yy and \u2208xy, terms in said two dimensional strain tensor are formed from HAADF-STEM images formed by scanning in a vertical, y-direction.
8. A method of mapping the strain in a crystalline sample, comprising:
forming a high angle annular dark field scanning transmission electron microscope (HAADF-STEM) image of said crystalline sample including at least two regions with different strain where a Fourier transform defractogram of said image includes (111) Bragg reflections by scanning in at least one scan direction;
selecting two independent Bragg reflections in said Fourier transform defractogram;
performing geometric phase analysis (GPA) with said two said independent Bragg reflections; and

forming a strain map of the sample for at least one term in a two dimensional strain tensor that is related to the strain in said scan direction.
9. The method of claim 8 where said scan direction is a horizontal, x-direction and where said term in said two dimensional strain tensor is at least one of horizontal related terms in said stress tensor, \u2208xx and \u2208yx.
10. The method of claim 8 where said scan direction is a vertical, y-direction and where said term in said two dimensional strain tensor is at least one of vertical related terms in said stress tensor, \u2208yy and \u2208xy.
11. The method of claim 8 where said crystalline sample is a MOS transistor and where said two regions include a channel region and at least one of a source, drain, and substrate region.
12. The method of claim 8 where said crystalline sample is a bipolar transistor and where said two regions include a base region and at least one of a emitter, collector, and substrate region.
13. A method of mapping each of the components of the strain tensor in a semiconductor device, comprising:
forming a first high angle annular dark field scanning transmission electron microscope (HAADF-STEM) image of said semiconductor device including at least two regions with different strain where a first Fourier transform defractogram of said first image includes (111) Bragg reflections by scanning in a horizontal direction;
selecting first and second independent Bragg reflections from said Fourier transform defractogram;
performing a first geometric phase analysis (GPA) with said first and second independent Bragg reflections; and

forming a first and second strain map for two components of said strain tensor related to horizontal strain;
forming a second HAADF-STEM image of said semiconductor device including said two regions with different strain where a second Fourier transform defractogram of said second HAADF-STEM image includes (111) Bragg reflections by scanning in a vertical direction;
selecting third and fourth independent Bragg reflections from said second Fourier transform defractogram;
performing a second GPA with said third and fourth independent Bragg reflections; and

forming third and fourth strain maps for two components of said strain tensor related to vertical strain.
14. The method of claim 13 where said semiconductor device is a MOS transistor and where said two regions include a channel region and at least one of a source, drain, and substrate region.
15. The method of claim 13 where said semiconductor device is a bipolar transistor and where said two regions include a base region and at least one of a emitter, collector, and substrate region.

1. A self-assembling peptide nanoparticle consisting of aggregates of a multitude of building blocks of formula (I) consisting of a continuous chain comprising a peptidic oligomerization domain D1, a linker segment L, and a peptidic oligomerization domain D2
D1-L-D2\u2003\u2003(I)
wherein D1 is a peptide having a tendency to form oligomers (D1)m of m subunits D1, D2 is a peptide having a tendency to form oligomers (D2)n of n subunits D2, m and n each is a figure between 2 and 10, with the proviso that m is not equal n and not a multiple of n, and n is not a multiple of m, L is a bond or a short linker segment, either D1 or D2 or both D1 and D2 is a coiled-coil oligomerization domain that incorporates one or more T- andor B-cell epitopes within the oligomerization domain, and wherein D1, D2 and L are optionally further substituted.
2. The peptide nanoparticle according to claim 1 wherein the coiled-coil oligomerization domain is consisting of heptad andor undecad repeats.
3. The peptide nanoparticle according to claim 1 wherein the peptidic oligomerization domain D1 at its N-terminal end andor the peptidic oligomerization domain D2 at its C-terminal end is substituted by one or more additional B- andor T-cell epitope, one or more other functional peptide or protein, or one or more additional hapten or other functional molecule.
4. The peptide nanoparticle according to claim 3 of the formulae S1-D1-L-D2, D1-L-D2-S2, or S1-D1-L-D2-S2, wherein S1 and S2 are peptidic substituents.
5. The peptide nanoparticle according to claim 3, consisting of identical building blocks D1-L-D2, wherein at least one of the identical building blocks carries one or more different substituent at the N-terminal end of D1 andor the C-terminal end of D2.
6. The peptide nanoparticle according to claim 1 wherein one of the oligomerization domains D1 and D2 is the pentamerization domain of the tryptophane zipper or a derivative thereof.
7. The peptide nanoparticle according to claim 1 wherein one of the oligomerization domains D1 and D2 is the tetramerization domain of tetrabrachion or a derivative thereof.
8. The peptide nanoparticle according to claim 1 wherein at least one of the epitopes is a CTL epitope.
9. The peptide nanoparticle according to claim 1 wherein at least one of the epitopes is a HTL epitope.
10. The peptide nanoparticle according claim 1 wherein at least one of the epitopes is a B-cell epitope.
11. The peptide nanoparticle according to claim 1 wherein the sequence D1-L-D2 comprises a series of optionally overlapping T- andor B-cell epitopes.
12. A composition comprising a peptide nanoparticle according to claim 1.
13. The composition of claim 12, wherein at least one of the B- or T-cell epitopes is selected from the group consisting of:
(a) an antigen suited to induce an immune response against bacteria;
(b) an antigen suited to induce an immune response against viruses;
(c) an antigen suited to induce an immune response against parasites;
(d) an antigen suited to induce an immune response against cancer cells;
(e) an antigen suited to induce an immune response against allergens;
(f) an antigen suited to induce an immune response against addictions;
(g) an antigen suited to induce an immune response against diseases and metabolic disorders;
(h) an antigen suited to induce an immune response in a farm animals; and
(i) an antigen suited to induce an immune response in a pet.
14. The composition of claim 12, wherein at least one of the B- or T-cell epitopes is selected from a protein of the pathogens causing diseases selected from the group consisting of Amoebiasis, Anthrax, Campylobacter infection, Chickenpox, Cholera, Dengue, Diphtheria, Encephalitis, Ebola, Influenza, Japanese Encephalitis, Leishmaniasis, Malaria, Measles, Meningococcal Disease, Mumps, Nosocomial infections, Pertussis, Pneumococcal Disease, Polio (Poliomyelitis), Rubella, Shingles, Shistosomiasis, Tetanus, Tick-Borne Encephalitis, Trichomoniasis, Trypanosomiasis, Tuberculosis, Typhoid, Varicella, and Yellow Fever.
15. The composition of claim 12, wherein at least one of the B- or T-cell epitopes is selected from a protein of the pathogens causing diseases selected from the group consisting of Campylobacter, Cytomegalovirus, Epstein-Barr Virus, FMDV, Haemophilus influenzae Type b, Helicobacter pylori, Hepatitis B Virus, Hepatitis C Virus, Hepatitis E Virus, Herpes Simplex Virus, Human Immunodeficiency Virus, Human Papillomavirus, Neisseria meningitidis, Pseudomonas aeruginosa, Staphylococcus aureus, Streptococcus pneumoniae, Respiratory Syncytial Virus, Rotavirus, Roundworm, Hookworm, and West Nile Virus.
16. The composition of claim 12, wherein at least one of the B- or T-cell epitopes is selected from the influenza proteins hemagglutinin andor M2.
17. The composition of claim 16, wherein the M2 B-cell epitope is the tetrameric form of the extracellular portion of this protein M2e attached to the N-terminal end of a tetrameric coiled-coil oligomerization domain D1.
18. The composition of claim 17, wherein the tetrameric oligomerization domain D1 is the tetrameric coiled-coil domain of tetrabrachion or a derivative thereof.
19-20. (canceled)
21. The composition of claim 12, wherein at least one of the B-cell epitopes is a sequence of between 8 and 48 residues that constitute a B cell epitope of the Plasmodium falciparum circumsporozoite (CS) protein said B cell epitope being comprised of two to about 12 repeats of the amino acid residue sequence Asn-Ala-Asn-Pro or permutations thereof.
22-25. (canceled)
26. The composition of claim 12, wherein at least one of the B-cell epitopes is a protein of HIV selected from the proteins gp41, gp120 or gp160.
27. The composition of claim 12, wherein at least one of the B-cell epitopes is a peptide of HIV selected from the binding sites of the neutralizing antibodies 2F5 andor 4E10 of gp41.
28. The composition of claim 12, wherein at least one of the B-cell epitopes is a peptide of HIV selected from the V3-loop of gp120 of HIV.
29-30. (canceled)
31. The composition of claim 12 wherein the B-cell epitope is an antigen suited to induce an immune response against addictions selected from the group consisting of opiates, marijuana, amphetamines, cocaine, barbiturates, glutethimide, methyprylon, chloral hydrate, methaqualone, benzodiazepines, LSD, nicotine, anticholinergic drugs, antipsychotic drugs, tryptamine, other psychomimetic drugs, sedatives, phencyclidine, psilocybine, volatile nitrite, and other drugs inducing physical dependence andor psychological dependence.
32-33. (canceled)
34. The composition of claim 12, wherein at least one of the B- or T-cell epitopes is selected from an antigen suited to induce an immune response against cancer cells of a type of cancer selected from Brain Cancer, Breast Cancer, Cervical Cancer, Colorectal Cancer, Esophageal Cancer, Glioblastoma, Leukemia (acute Myelogenous and chronic Myeloid), Liver cancer, Lung Cancer (Non-Small-Cell Lung Cancer, Small-Cell Lung Cancer), Lymphoma (Non-Hodgkin’s Lymphoma), Melanoma, Ovarian Cancer, Pancreatic Cancer, Prostate Cancer, and Renal Cancer.
35-36. (canceled)
37. The composition of claim 12, wherein at least one of the B-cell epitopes is the A\u03b2-peptide or a fragment thereof comprising at least the sequence of 6 amino acids starting with the N-terminal amino acids.
38. The composition of claim 12, wherein at least one of the B-cell epitopes is angiotensin I or angiotensin II.
39. The composition of claim 12, wherein at least one of the B-cell epitopes is grehlin.
40. The composition of claim 12, wherein at least one of the B-cell epitopes is TNF\u03b1 or a fragment thereof comprising at least the sequence of 20 amino acids starting with the 4th N-terminal amino acid of TNF\u03b1.
41. A method of vaccinating a human or non-human animal, which comprises administering an effective amount of a peptide nanoparticle according to claim 1 to a subject in need of such vaccination.
42. A monomeric building block of formula (I) consisting of a continuous chain comprising a peptidic oligomerization domain D1, a linker segment L, and a peptidic oligomerization domain D2
D1-L-D2\u2003\u2003(I)
wherein D1 is a peptide having a tendency to form oligomers (D1)m of m subunits D1, D2 is a peptide having a tendency to form oligomers (D2)n of n subunits D2, m and n each is a figure between 2 and 10, with the proviso that m is not equal n and not a multiple of n, and n is not a multiple of m, L is a bond or a short linker segment, either D1 or D2 or both D1 and D2 is a coiled-coil oligomerization domain that incorporates one or more T- andor B-cell epitopes within the oligomerization domain, and wherein D1, D2 and L are optionally further substituted.

The claims below are in addition to those above.
All refrences to claim(s) which appear below refer to the numbering after this setence.

1. A laboratory autography phosphorescent marking pen capable of delivering a low viscosity phosphorescent marking ink comprising a suspension of phosphor particles having an average particle size of between 10 and 40 microns, and whose afterglow half-life is less than 5 minutes, wherein said marking pen further comprises a high porosity nib whose ink flow channels are of a sufficient size to allow said phosphor particles suspended in said ink to flow by capillary transport through said channels onto an ink receiving substrate material.
2. The phosphorescent marking pen of claim 1 wherein the phosphorescent marking ink has a viscosity of between 10 and 200 centipoise at 25\xb0 C.
3. The phosphorescent marking pen of claim 2 wherein the phosphorescent marking ink has a viscosity of between 35 and 50 centipoise at 25\xb0 C.
4. The phosphorescent marking pen of claim 1 wherein said marking pen comprises a reservoir that contains said marking ink together with at least one agitator element that allows said phosphor particles to be resuspended in said marking ink upon manual shaking of said marking pen.
5. The phosphorescent marking pen of claim 1 wherein said ink further comprises an amount of colorant that is sufficient for said ink to be visible while writing, said colorant being a white or colored pigment or dye.
6. The phosphorescent marking pen of claim 5 wherein said colorant is one or more materials selected from the group consisting of green dye, yellow dye, green pigment and yellow pigment.
7. The phosphorescent marking pen of claim 1 wherein the afterglow half-life of said phosphorescent marking ink, after drying on said substrate material, is less than 3 minutes.
8. The phosphorescent marking pen of claim 1 wherein said phosphor particles having an average particle size of between 10 and 25 microns.
9. The phosphorescent marking pen of claim 1 wherein said phosphor particles are zinc sulfide-based particles.
10. The phosphorescent marking pen of claim 9 wherein said zinc sulfide-based particles are copper-doped zinc sulfide-based particles.
11. The phosphorescent marking pen of claim 1 wherein said phosphor particles are a hexagonal Wurtzite crystalline form of zinc sulfide doped with various trace metals.
12. The phosphorescent marking pen of claim 1 wherein said a high porosity fiber-type writing nib is fabricated from fibers selected from the group consisting of polyethylene fibers, polypropylene fibers, acrylic fibers, polyester fibers and nylon fibers.
13. The phosphorescent marking pen of claim 1, wherein said writing nib is formed into a point.
14. The phosphorescent marking pen of claim 13, wherein the point of said writing nib is approximately 0.4-3 mm in diameter.
15. The phosphorescent marking pen of claim 14, wherein said writing nib is 0.6-1.5 mm in diameter.
16. The phosphorescent marking pen of claim 1 wherein the liquid vehicle in said low viscosity phosphorescent marking ink is selected from the group consisting of petroleum and water-based vehicles.
17. The phosphorescent marking ink of claim 1 wherein said ink contains between 5% and 30% by weight of said phosphor particles.
18. The phosphorescent marking pen of claim 1 wherein said marking pen comprises a reservoir that contains said marking ink, and further comprises an ink flow valve positioned between said reservoir and said writing nib.
19. A method of using a laboratory autography marking pen comprising the steps of:
writing notations on a substrate material using the laboratory autography marking pen and phosphorescent marking ink of claim 1;
exposing the annotated substrate material to visible or ultraviolet light to excite the phosphor particles in said marking ink;
placing said annotated substrate material into contact with X-ray film or other photo-detection surface for a period of time sufficient for the notations to be registered on said photo-detection surface; and
processing said photo-detection surface using a procedure suitable for visualizing said notations.
20. The method of claim 19, wherein said phosphorescent marking ink has a viscosity of between 10 and 200 centipoise at 25\xb0 C., said phosphor particles are zinc sulfide-based particles, and wherein said writing nib is formed into a point of approximately 0.4-3 mm in diameter.