What is claimed is:
1. A method for identifying memory cells storing data in a memory device, the method comprising:
(a) providing a set of memory cells in a memory device, the set of memory cells storing an identification pattern;
(b) overwriting some of the memory cells storing the identification pattern with data; and
(c) identifying the memory cells storing the data by identifying the memory cells that are adjacent to the memory cells storing the identification pattern.
2. The method of claim 1, wherein (c) comprises identifying the memory cells that are within a predetermined number of memory cells adjacent to the memory cells storing the identification pattern.
3. The method of claim 1, wherein (c) comprises identifying the memory cells that are between two sets of memory cells storing the identification pattern.
4. The method of claim 1, wherein (c) comprises identifying the memory cells that are between a set of memory cells storing a predetermined pattern of data and a set of memory cells storing the identification pattern.
5. The method of claim 1, wherein the memory cells that are overwritten in (b) are between memory cells storing the identification pattern and memory cells storing previously-stored data.
6. The method of claim 1, wherein the memory cells storing the identification pattern are all in an un-programmed logic state.
7. The method of claim 1, wherein some of the memory cells storing the identification pattern are in an un-programmed logic state and other memory cells storing the identification pattern are in a programmed logic state.
8. The method of claim 1, wherein the data comprises a description of a file stored in the memory device.
9. The method of claim 1, wherein the data comprises a pointer to a file stored in the memory device.
10. The method of claim 1, wherein the data comprises an entry to a calendar application run by a data storage system coupled with the memory device.
11. The method of claim 1, wherein the data comprises a picture stored by a picture editing application run by a data storage system coupled with the memory device.
12. The method of claim 1, wherein the memory device is logically organized into a plurality of blocks, each block comprising at least one line.
13. The method of claim 12, wherein a line comprises a minimum number of memory cells that can be written into during a write operation.
14. The method of claim 1, wherein the memory device comprises a write-once memory device.
15. The method of claim 1, wherein the memory device comprises a three-dimensional write-once memory device.
16. A method for identifying memory cells storing data in a memory device, the method comprising:
(a) storing data in a first set of memory cells of a memory device;
(b) storing an identifier in a second set of memory cells adjacent to the first set of memory cells, the identifier indicating which memory cells adjacent to the identifier store the data; and
(c) identifying the first set of memory cells using the identifier.
17. The method of claim 16, wherein the identifier is stored at an end of the stored data.
18. The method of claim 16, wherein the data is stored before and after the identifier.
19. The method of claim 16, wherein the identifier is fixed.
20. The method of claim 16, wherein the identifier is dynamic.
21. The method of claim 16, wherein the identifier indicates whether the data stored before the identifier is valid.
The claims below are in addition to those above.
All refrences to claim(s) which appear below refer to the numbering after this setence.
We claim:
1. A glucose biosensor for in vivo or in vitro use comprising:
a) at least one mutated binding protein and at least one reporter group attached thereto such that said reporter group provides a detectable and reversible signal change when said mutated binding protein is exposed to varying glucose concentrations;
wherein said detectable and reversible signal change is related to said varying concentrations.
2. The biosensor of claim 1 wherein said mutated binding protein is glucosegalactose binding protein.
3. The biosensor of claim 1 wherein said binding protein has one amino acid substitution.
4. The biosensor of claim 1 wherein said binding protein has at least two amino acid substitutions.
5. The biosensor of claim 1 wherein said binding protein has at least three amino acid substitutions.
6. The biosensor of claim 3 wherein said one amino acid substitution is selected from the group consisting of a cysteine at position 11, a cysteine at position 14, a cysteine at position 19, a cysteine at position 43, a cysteine at position 74, a cysteine at position 107, a cysteine at position 110, a cysteine at position 112, a cysteine at position 113, a cysteine at position 137, a cysteine at position 149, a cysteine at position 213, a cysteine at position 216, a cysteine at position 238, a cysteine at position 287, and a cysteine at position 292.
7. The biosensor of claim 6 wherein said binding protein has at least one histidine tag.
8. The biosensor of claim 4 wherein said at least two amino acid substitutions are selected from the group consisting of a cysteine at position 112 and a serine at position 238, a cysteine at position 149 and a serine at position 238, a cysteine at position 152 and a cysteine at position 182, a cysteine at position 152 and a serine at position 213, a cysteine at position 213 and a cysteine at position 238, a cysteine at position 149 and an arginine at position 213.
9. The biosensor of claim 8 wherein said binding protein has at least one histidine tag.
10. The biosensor of claim 5 wherein said at least three amino acid substitutions are selected from the group consisting of a cysteine at position 149 and a serine at position 213 and a serine at position 238, and a cysteine at position 149 and an arginine at position 213 and a serine at position 238.
11. The biosensor of claim 10 wherein said binding protein has at least one histidine tag.
12. The biosensor of claim 1 wherein said reporter group is a luminescent label.
13. The biosensor of claim 12 wherein said luminescent label has an excitation wavelength of more than about 600 nanometers.
14. The biosensor of claim 12 wherein said luminescent label has an emission wavelength of more than about 600 nanometers.
15. The biosensor of claim 12 wherein said luminescent label is covalently coupled to said at least one glucosegalactose binding protein.
16. The biosensor of claim 15 wherein said luminescent label is covalently coupled to said at least one glucosegalactose binding protein by reaction with a member selected from the group consisting of fluorescein, coumarins, rhodamines, 5-TMRIA (tetramethylrhodamine-5-iodoacetamide), Quantum Red, Texas Red, Cy3, N-((2-iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenzoxadiazole (IANBD), 6-acryloyl-2-dimethylaminonaphthalene (acrylodan), pyrene, Lucifer Yellow, Cy5, Dapoxyl (2-bromoacetamidoethyl)sulfonamide, (N-(4,4-difluoro-1,3,5,7-tetramethyl-4-bora-3a,4a-diaza-s-indacene-2-yl)iodoacetamide (Bodipy507545 IA), N-(4,4-difluoro-5,7-diphenyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl)-N-iodoacetylethylenediamine (BODIPY 530550 IA), 5-((((2-iodoacetyl)amino)ethyl) amino)naphthalene-1-sulfonic acid (1,5-IAEDANS), and carboxy-X-rhodamine, 56-iodoacetamide (XRIA 5,6).
17. A method for glucose detection comprising:
b) providing at least one mutated glucosegalactose binding protein and at least one reporter group attached thereto;
c) exposing said mutated glucosegalactose binding protein to varying glucose concentrations;
d) detecting a detectable and reversible signal change from said reporter group wherein said detectable and reversible signal change corresponds to said varying glucose concentrations.
18. The method of claim 17 wherein said detecting is continuous, programmed, episodic, or combinations thereof.
19. The method of claim 17 wherein said mutated glucosegalactose binding protein is selected from bacterial periplasmic binding proteins.
20. The method of claim 17 wherein said detecting of detectable and reversible signal changes from said reporter group of varying glucose concentrations is in vivo.
21. The method of claim 17 wherein said binding protein has one amino acid substitution.
22. The method of claim 17 wherein said binding protein has at least two amino acid substitutions.
23. The method of claim 17 wherein said binding protein has at least three amino acid substitutions.
24. The method of claim 21 wherein said one amino acid substitution is selected from the group consisting of a cysteine at position 11, a cysteine at position 14, a cysteine at position 19, a cysteine at position 43, a cysteine at position 74, a cysteine at position 107, a cysteine at position 110, a cysteine at position 112, a cysteine at position 113, a cysteine at position 137, a cysteine at position 149, a cysteine at position 213, a cysteine at position 216, a cysteine at position 238, a cysteine at position 287, and a cysteine at position 292.
25. The method of claim 24 wherein said glucosegalactose binding protein has at least one histidine tag.
26. The method of claim 22 wherein said glucosegalactose binding protein has at least two amino acid substitutions selected from the group consisting of a cysteine at position 112 and a serine at position 238, a cysteine at position 149 and a serine at position 238, a cysteine at position 152 and a cysteine at position 182, a cysteine at position 152 and a serine at position 213, a cysteine at position 213 and a cysteine at position 238, a cysteine at position 149 and an arginine at position 213.
27. The method of claim 26 wherein said glucosegalactose binding protein has at least one histidine tag.
28. The method of claim 23 wherein said glucosegalactose binding protein has at least three amino acid substitutions selected from the group consisting of a cysteine at position 149 and a serine at position 213 and a serine at position 238, and a cysteine at position 149 and an arginine at position 213 and a serine at position 238.
29. The method of claim 28 wherein said glucosegalactose binding protein has at least one histidine tag.
30. The method of claim 17 wherein said at least one reporter group is a luminescent label.
31. The method of claim 30 wherein said luminescent label has an excitation wavelength of more than about 600 nanometers.
32. The method of claim 30 wherein said luminescent label has an emission wavelength of more than about 600 nanometers.
33. The method of claim 30 wherein said luminescent label is covalently coupled to said at least one glucosegalactose binding protein by reaction with said at least one mutated binding protein and a member selected from the group consisting of fluorescein, coumarins, rhodamines, 5-TMRIA (tetramethylrhodamine-5-iodoacetamide), Quantum Red, Texas Red, Cy3, N-((2-iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenzoxadiazole (IANBD), 6-acryloyl-2-dimethylaminonaphthalene (acrylodan), pyrene, Lucifer Yellow, Cy5, Dapoxyl (2-bromoacetamidoethyl)sulfonamide, (N-(4,4-difluoro-1,3,5,7-tetramethyl-4-bora-3a,4a-diaza-s-indacene-2-yl)iodoacetamide (Bodipy507545 IA), N-(4,4-difluoro-5,7-diphenyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl)-N-iodoacetylethylenediamine (BODIPY 530550 IA), 5-((((2-iodoacetyl)amino)ethyl) amino)naphthalene-1-sulfonic acid (1,5-IAEDANS), and carboxy-X-rhodamine, 56-iodoacetamide (XRIA 5,6).
34. A composition comprising:
a mutated glucosegalactose binding protein having at least one amino acid substitution selected from the group consisting of a cysteine at position 11, a cysteine at position 14, a cysteine at position 19, a cysteine at position 43, a cysteine at position 74, a cysteine at position 107, a cysteine at position 110, a cysteine at position 112, a cysteine at position 113, a cysteine at position 137, a cysteine at position 149, a cysteine at position 213, a cysteine at position 216, a cysteine at position 238, a cysteine at position 287, and a cysteine at position 292.
35. The composition of claim 34 wherein said mutated glucosegalactose binding protein has at least one histidine tag.
36. The composition of claim 34 wherein said mutated glucosegalactose binding protein further has at least one reporter group.
37. The composition of claim 36 wherein at least one reporter group is a luminescent label.
38. The composition of claim 37 wherein said luminescent label has an excitation wavelength of more than about 600 nanometers.
39. The composition of claim 37 wherein said luminescent label has an emission wavelength of more than about 600 nanometers.
40. The composition of claim 37 wherein said luminescent label is covalently coupled to said at least one glucosegalactose binding protein by reaction with said at least one mutated binding protein and a member selected from the group consisting of fluorescein, coumarins, rhodamines, 5-TMRIA (tetramethylrhodamine-5-iodoacetamide), Quantum Red, Texas Red, Cy3, N-((2-iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenzoxadiazole (IANBD), 6-acryloyl-2-dimethylaminonaphthalene (acrylodan), pyrene, Lucifer Yellow, Cy5, Dapoxyl (2-bromoacetamidoethyl)sulfonamide, (N-(4,4-difluoro-1,3,5,7-tetramethyl-4-bora-3a,4a-diaza-s-indacene-2-yl)iodoacetamide (Bodipy507545 IA), N-(4,4-difluoro-5,7-diphenyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl)-N-iodoacetylethylenediamine (BODIPY 530550 IA), 5-((((2-iodoacetyl)amino)ethyl) amino)naphthalene-1-sulfonic acid (1,5-IAEDANS), and carboxy-X-rhodamine, 56-iodoacetamide (XRIA 5,6).
41. A composition comprising:
a mutated glucosegalactose binding protein having at least two amino acid substitutions selected from the group consisting of a cysteine at position 112 and a serine at position 238, a cysteine at position 149 and a serine at position 238, a cysteine at position 152 and a cysteine at position 182, a cysteine at position 152 and a serine at position 213, a cysteine at position 213 and a cysteine at position 238, a cysteine at position 149 and an arginine at position 213, and a cysteine at position 149 and a serine at position 213 and a serine at position 238, and a cysteine at position 149 and an arginine at position 213 and a serine at position 238.
42. The composition of claim 41 wherein said mutated glucosegalactose binding protein has at least one histidine tag.
43. The composition of claim 41 wherein said mutated glucosegalactose binding protein further has at least one reporter group.
44. The composition of claim 43 wherein at least one reporter group is a luminescent label.
45. The composition of claim 44 wherein said luminescent label has an excitation wavelength of more than about 600 nanometers.
46. The composition of claim 44 wherein said luminescent label has an emission wavelength of more than about 600 nanometers.
47. The composition of claim 44 wherein said luminescent label is covalently coupled to said at least one glucosegalactose binding protein by reaction with said at least one mutated binding protein and a member selected from the group consisting of fluorescein, coumarins, rhodamines, 5-TMRIA (tetramethylrhodamine-5-iodoacetamide), Quantum Red, Texas Red, Cy3, N-((2-iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenzoxadiazole (IANBD), 6-acryloyl-2-dimethylaminonaphthalene (acrylodan), pyrene, Lucifer Yellow, Cy5, Dapoxyl (2-bromoacetamidoethyl)sulfonamide, (N-(4,4-difluoro-1,3,5,7-tetramethyl-4-bora-3a,4a-diaza-s-indacene-2-yl)iodoacetamide (Bodipy507545 IA), N-(4,4-difluoro-5,7-diphenyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl)-N-iodoacetylethylenediamine (BODIPY 530550 IA), 5-((((2-iodoacetyl)amino)ethyl) amino)naphthalene-1-sulfonic acid (1,5-IAEDANS), and carboxy-X-rhodamine, 56-iodoacetamide (XRIA 5,6).