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NMR- Data [1] of valine:

Valin Atom Typ chemical shift [ppm]1 Random Coil
chem. shift 3
Random Coil
chem. shift 4
average σ5 entries2
H H  8.28 0.687 55381  8.03  8.02
H  4.172 0.646 42441  4.12  4.44
H  1.976 0.474 39770  2.08  2.06
Hγ1 H  0.82 0.35 39325  0.94  0.97
Hγ2 H  0.80 0.462 38582  0.93  0.92
C C  175.638 3.242 35667  176.3  174.9
C  62.529 2.903 48856  62.2  59.8
C  32.746 2.103 45470  32.9  32.6
Cγ1 C  21.527 1.897 33534  21.1  20.9
Cγ2 C  21.324 2.043 32334  20.3  20.1
N N  121.205 8.171 52437  119.2  120.5
proportion of proteins pK2 COOH pK1COOH isoelectrical point pK1NH2 pK2NH2
 6.9%  –  2.30  5.96  9.60  –
CAS- number molar mass formula solubility melting point density
  • 72-18-4 (L-Enantiomer)
  • 640-68-6 (D-Enantiomer)
  • 516-06-3 (DL-Enantiomer mixture)
 117.15 g·mol−1  C5H11NO2
  • in water (85 g·l−1 at 20 °C)
  • unsoluble in Diethylether, Aceton and Benzol
 295–300 °C 1.23 g·cm−3

1 Depending on the type of atom it was 1H, 13C or 15N chemical shift. 1H und 13C relative to TMS and 15N relative to liquid ammonia

2 Number of individual chemical shift data for averaging according to [2]

3 with Alanine as neighborhood in the hexapeptide Gly-Gly-X-Ala-Gly-Gly [3]

4 with Proline as neighborhood in the hexapeptide Gly-Gly-X-Pro-Gly-Gly [3]

5 standard deviation


3D- Modell

sources:

[1] “BioMagResBank”, Eldon L. Ulrich; Hideo Akutsu; Jurgen F. Doreleijers; Yoko Harano; Yannis E. Ioannidis; Jundong Lin; Miron Livny; Steve Mading; Dimitri Maziuk; Zachary Miller; Eiichi Nakatani; Christopher F. Schulte; David E. Tolmie; R. Kent Wenger; Hongyang Yao; John L. Markley; Nucleic Acids Research 36, D402-D408 (2008) doi: 10.1093/nar/gkm957

[2] http://www.bmrb.wisc.edu/ last visit march 2017

[3] David S. Wishart, Colin G. Bigam, Arne Holm, Robert S. Hodges, Brian D. Sykes; Journal of Biomolecular NMR
January 1995, Volume 5, Issue 1, pp 67-81 doi:10.1007/BF00227471

[4] Wikipedia http://de.wikipedia.org/wiki/Aminos%C3%A4uren (last visit january 2014)

[5] Wikipedia http://de.wikipedia.org/wiki/Alanin (las visit Januar 2014)proportion of proteinsproportion of proteins

3D Mol: Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

NMR- data [1] of tyrosine:

Tyrosin Atom Atomtyp chemical shift [ppm]1 Random Coil
chem. shift3
Random Coil
chem. shift4
average standard deviation entries2
H H  8.304 0.739 25862  8.12  8.10
H  4.615 0.569 19854  4.55  4.84
Hβ2 H  2.893 0.487 18588  3.03  3.05
Hβ3 H  2.831 0.505 18171  2.98  2.89
Hδ1 H  6.913 0.387 16267  7.14  7.15
Hδ2 H  6.911 0.394 13742  7.14  7.15
Hε1 H  6.69 0.319 15485  6.84  6.86
Hε2 H  6.689 0.330 13214  6.84  6.86
H  9.162 2.201 363  –  –
C C  175.316 4.705 15592  175.9  174.8
C  58.127 2.613 21816  57.9  55.8
C  39.324 2.729 20343  38.8  38.3
C  128.403  12.173  266  130.6  130.7
Cδ1 C  132.866  16.948 9563  133.3  133.5
Cδ2 C  133.072  20.211 6542  133.3  133.5
Cε1 C  117.734 3.795 9490  118.2  118.2
Cε2 C  117.779 3.031 6493  118.2  118.2
C  154.991  16.034  216  157.3  157.3
N N  120.877  14.047 23572  120.3  120.8
proportion in proteins pK2 COOH pK1COOH isoelectrical point pK1NH2 pK2NH2
 3.5%  10.07 (Ph-OH)  2.20  5.66  9.11  –
CAS- number molar mass formula density melting point solubility
  • 60-18-4 (L-Tyrosine)
  • 556-02-5 (D-Tyrosine)
  • 556-40-6 (DL-Tyrosine)
 181.19 g·mol−1  C9H11NO3  1.46 g·cm−3 (25 °C) 342–344 °C (decomposition)
  • good in acids and bases
  • bad in water (0.38 g·l−1 at 20 °C)
  • unsoluble in Ethanol, Ether and Aceton

1 Depending on the type of atom it was 1H, 13C or 15N chemical shift. 1H und 13C relative to TMS and 15N relative to liquid ammonia

2 Number of individual chemical shift data for averaging according to [2]

3 with Alanine as neighborhood in the hexapeptide Gly-Gly-X-Ala-Gly-Gly [3]

4 with Proline as neighborhood in the hexapeptide Gly-Gly-X-Pro-Gly-Gly [3]


3D- Modell

sources:

[1] “BioMagResBank”, Eldon L. Ulrich; Hideo Akutsu; Jurgen F. Doreleijers; Yoko Harano; Yannis E. Ioannidis; Jundong Lin; Miron Livny; Steve Mading; Dimitri Maziuk; Zachary Miller; Eiichi Nakatani; Christopher F. Schulte; David E. Tolmie; R. Kent Wenger; Hongyang Yao; John L. Markley; Nucleic Acids Research 36, D402-D408 (2008) doi: 10.1093/nar/gkm957

[2] http://www.bmrb.wisc.edu/ last visit march 2017

[3] David S. Wishart, Colin G. Bigam, Arne Holm, Robert S. Hodges, Brian D. Sykes; Journal of Biomolecular NMR
January 1995, Volume 5, Issue 1, pp 67-81 doi:10.1007/BF00227471

[4] Wikipedia http://de.wikipedia.org/wiki/Aminos%C3%A4uren (last visit january 2014)

[5] Wikipedia http://de.wikipedia.org/wiki/Alanin (las visit Januar 2014)proportion of proteinsproportion of proteins

3D Mol: Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

NMR- data [1] of tryptophan:

Tryptophan Atom Atomtyp chemical shift [ppm]1 Random Coil
chem. shift 3
Random Coil
chem. shift 4
average standard deviatiom entries2
H H  8.28 0.93 10154  8.25  8.09
H  4.682 0.54 7779  4.66  4.99
Hβ2 H  3.174 0,355 7384  3.29  3.32
Hβ3 H  3.112 0.374 7181  3.27  3.16
Hδ1 H  7.126 0,365 6628  7.27  7.25
Hε1 H  10.074 0.718 7182  –  –
Hε3 H  7.284 0.536 5849  7.65  7.69
Hζ2 H  7.26 0.43 6270  7.50  7.51
Hζ3 H  6.836 0.497 5657  7.18  7.19
Hη2 H  6.943 0.478 5797  7.25  7.27
C C  176.127 3.89 6074  176.1  174.8
C  57.707 2.987 8367  57.5  55.7
C  30.10 2.941 7908  29.6  28.9
C  109.96 8.958 205  111.2  111.3
Cδ1 C  126.283 4.345 4114  127.4  127.3
Cδ2 C  128.394 2.94 141  129.5  129.6
Cε2 C  138.222 6.987 178  138.7  138.8
Cε3 C  120.128 5.224 3486  122.2  122.2
Cζ2 C  114.032 4.254 3943  114.7  114.7
Cζ3 C  121.095 4.868 3524  124.8  124.8
Cη2 C  123.516 5.066 3680  121.0  120.9
N N  121.664 4.846 9099  121.3  122.2
Nε1 N  129.214 3.909 5795  –  –
proportion in proteins pK2 COOH pK1COOH isoelectrical
point
pK1NH2 pK2NH2
 1.1%  –  2.15  5.64  9.12  –
CAS- number molar Mass formula density melting point solubility
  • 73-22-3 (L-Tryptophan)
  • 153-94-6 (D-Tryptophan)
  • 54-12-6 (DL-Tryptophan)
 204,23 g·mol−1  C11H12N2O2
  • 290−295 °C (decomposition)
  • 257 °C (Hydrochlorid)
  • bad in cold water (10 g·l−1 at 20 °C,
    13,4 g·l−1 bei 25 °C) , better in hot water
  • bad in cold Ethanol, better in warm Ethanol
  • unsoluble in Chloroform

1 Depending on the type of atom it was 1H, 13C or 15N chemical shift. 1H und 13C relative to TMS and 15N relative to liquid ammonia

2 Number of individual chemical shift data for averaging according to [2]

3 with Alanine as neighborhood in the hexapeptide Gly-Gly-X-Ala-Gly-Gly [3]

4 with Proline as neighborhood in the hexapeptide Gly-Gly-X-Pro-Gly-Gly [3]


3D- Modell

sources:

[1] “BioMagResBank”, Eldon L. Ulrich; Hideo Akutsu; Jurgen F. Doreleijers; Yoko Harano; Yannis E. Ioannidis; Jundong Lin; Miron Livny; Steve Mading; Dimitri Maziuk; Zachary Miller; Eiichi Nakatani; Christopher F. Schulte; David E. Tolmie; R. Kent Wenger; Hongyang Yao; John L. Markley; Nucleic Acids Research 36, D402-D408 (2008) doi: 10.1093/nar/gkm957

[2] http://www.bmrb.wisc.edu/ last visit march 2017

[3] David S. Wishart, Colin G. Bigam, Arne Holm, Robert S. Hodges, Brian D. Sykes; Journal of Biomolecular NMR
January 1995, Volume 5, Issue 1, pp 67-81 doi:10.1007/BF00227471

[4] Wikipedia http://de.wikipedia.org/wiki/Aminos%C3%A4uren (last visit january 2014)

[5] Wikipedia http://de.wikipedia.org/wiki/Alanin (las visit Januar 2014)proportion of proteinsproportion of proteins

3D Mol: Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

NMR- data [1] of threonine:

Threonin Atom Atomtyp chemical shift [ppm]1 Random Coil
chem. shift3
Random Coil
chem. shift 4
average standard deviation entrie2
H H  8.244 1.139 44831  8.15  8.15
H  4.458 0.556 34443  4.35  4.61
H  4.172 0.837 31798  4.24  4.11
Hγ1 H  5.311 1.322 1227  –  –
Hγ2 H  1.139 0.331 31493  1.21  1.23
C C  174.464 4.246 27922  174.7  173.2
C  62.245 2.658 38914  61.8  59.8
C  69.599 6.601 36242  69.8  69.8
Cγ2 C  21.591 1.984 25736  21.5  21.4
N N  115.489 6.833 41840  113.6  116.0
proportion in proteins pK2 COOH pK1COOH isoelectrical
point
pK1NH2 pK2NH2
 6.0%  –  2.1  5.6  9.12  –
CAS- number molar mass formula density melting point solubility
  • 72-19-5 (L-Threonine)
  • 632-20-2 (D-Threonine)
  • 80-68-2 (DL-Threonine)
  • 28954-12-3 (Lallo-Threonine)
  • 24830-94-2 (Dallo-Threonine)
 119,12 g·mol−1  C4H9NO3  255–257 °C (decomposition)(L-Threonine)  not good in water (90 g·l−1 at 20 °C), unsoluble in organic solvents

1 Depending on the type of atom it was 1H, 13C or 15N chemical shift. 1H und 13C relative to TMS and 15N relative to liquid ammonia

2 Number of individual chemical shift data for averaging according to [2]

3 with Alanine as neighborhood in the hexapeptide Gly-Gly-X-Ala-Gly-Gly [3]

4 with Proline as neighborhood in the hexapeptide Gly-Gly-X-Pro-Gly-Gly [3]


3D- Modell

sources:

[1] “BioMagResBank”, Eldon L. Ulrich; Hideo Akutsu; Jurgen F. Doreleijers; Yoko Harano; Yannis E. Ioannidis; Jundong Lin; Miron Livny; Steve Mading; Dimitri Maziuk; Zachary Miller; Eiichi Nakatani; Christopher F. Schulte; David E. Tolmie; R. Kent Wenger; Hongyang Yao; John L. Markley; Nucleic Acids Research 36, D402-D408 (2008) doi: 10.1093/nar/gkm957

[2] http://www.bmrb.wisc.edu/ last visit march 2017

[3] David S. Wishart, Colin G. Bigam, Arne Holm, Robert S. Hodges, Brian D. Sykes; Journal of Biomolecular NMR
January 1995, Volume 5, Issue 1, pp 67-81 doi:10.1007/BF00227471

[4] Wikipedia http://de.wikipedia.org/wiki/Aminos%C3%A4uren (last visit january 2014)

[5] Wikipedia http://de.wikipedia.org/wiki/Alanin (las visit Januar 2014)proportion of proteinsproportion of proteins

3D Mol: Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

NMR- data [1] of serine:

Serin Atom Atomtyp chemical shift [ppm]1 Random Coil
chem. shift 3
Random Coil
chem. shift 4
Mittelwert Standardabweichung Datenbasis2
H H  8.279 0.615 50449  8.31  8.26
H  4.483 0.497 39760  4.47  4.78
Hβ2 H  3.868 0.279 36618  3.89  3.85
Hβ3 H  3.841 0.296 33894  3.87  3.85
H  5.518 1.205 678
C C  174.601 3.204 32500  174.6  173.1
C  58.716 2.219 45339  58.3  56.4
C  63.713 5.383 42264  63.8  63.3
N N  116.28 3.93  42792  115.7  116.6
proportion of proteins pK2 COOH pK1COOH isoelectrical
point
pK1NH2 pK2NH2
 7.1%  –  2.21  5.68  9.15  –
CAS- number molar mass formula density melting point solubility
  • 56-45-1 (L-Serine)
  • 312-84-5 (D-Serine)
  • 302-84-1 (DL-Serine)
 105,09 g·mol−1  C3H7NO3  215–225 °C
  • good in water (360 g·l−1 at 20 °C)
  • not soluble  in diethylether and ethanol

1 Depending on the type of atom it was 1H, 13C or 15N chemical shift. 1H und 13C relative to TMS and 15N relative to liquid ammonia

2 Number of individual chemical shift data for averaging according to [2]

3 with Alanine as neighborhood in the hexapeptide Gly-Gly-X-Ala-Gly-Gly [3]

4 with Proline as neighborhood in the hexapeptide Gly-Gly-X-Pro-Gly-Gly [3]


3D- Modell

sources:

[1] “BioMagResBank”, Eldon L. Ulrich; Hideo Akutsu; Jurgen F. Doreleijers; Yoko Harano; Yannis E. Ioannidis; Jundong Lin; Miron Livny; Steve Mading; Dimitri Maziuk; Zachary Miller; Eiichi Nakatani; Christopher F. Schulte; David E. Tolmie; R. Kent Wenger; Hongyang Yao; John L. Markley; Nucleic Acids Research 36, D402-D408 (2008) doi: 10.1093/nar/gkm957

[2] http://www.bmrb.wisc.edu/ last visit march 2017

[3] David S. Wishart, Colin G. Bigam, Arne Holm, Robert S. Hodges, Brian D. Sykes; Journal of Biomolecular NMR
January 1995, Volume 5, Issue 1, pp 67-81 doi:10.1007/BF00227471

[4] Wikipedia http://de.wikipedia.org/wiki/Aminos%C3%A4uren (last visit january 2014)

[5] Wikipedia http://de.wikipedia.org/wiki/Alanin (las visit Januar 2014)proportion of proteinsproportion of proteins

3D Mol: Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829