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laiz [17]
3 years ago
5

Nitrogen fixation is a natural process by which inert or unreactive forms of nitrogen are transformed into usable nitrogen. why

is this process important to life
Biology
2 answers:
balu736 [363]3 years ago
8 0

Answer:

Because through them plants are able to supply their nitrogen needs and provide this element to humans and other animals whose nitrogen is essential.

Explanation:

Biological nitrogen fixation (BNF) is considered, after photosynthesis, the most important biological process on the planet. It is based on the fact that some microorganisms, known as diazotrophic, are able to break the bond that joins the two atoms of atmospheric nitrogen (N2) into ammonia (NH3), which is assimilable by plants. If the association between these microorganisms and plants is efficient, the fixed N can supply the needs of the plant, eliminating the use of nitrogen fertilizers and thus offering economic and ecological advantages. In addition, through food, plants provide nitrogen to humans and other animals.

Kitty [74]3 years ago
7 0
Nitrogen fixation is a natural process by which inert or unreactive forms of nitrogen are transformed 
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Number of different amino acids that make up all proteins
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Answer:

List of the 20 Amino Acids

Amino Acid 3-Letter Abbreviation 1-Letter Abbreviation Class of Amino Acid (Side Chain) Hydrophobicity Index (100 being extremely hydrophobic, 0 being neutral, and -55 being hydrophilic) Structure pKa of COOH group pKa of NH3+ group pKa of R group Molecular Weight [g/mol] alpha helix beta sheet Reverse turn

Glycine Gly G Aliphatic, nonpolar Neutral (0 at pH = 2; 0 at pH = 7)

2.4 9.8 -- 75.07 0.43 0.58 1.77

Alanine Ala A Aliphatic, nonpolar Hydrophobic (47 at pH = 2; 41 at pH = 7)

2.4 9.9 -- 89.1 1.41 0.72 0.82

Valine Val V Aliphatic, nonpolar Very Hydrophobic (79 at pH = 2; 76 at pH = 7)

2.3 9.7 -- 117.15 0.90 1.87 0.41

Leucine Leu L Aliphatic, nonpolar Very Hydrophobic (100 at pH = 2; 97 at pH = 7)

2.3 9.7 -- 131.18 1.34 1.22 0.57

Isoleucine Ile I Aliphatic, nonpolar Very Hydrophobic (100 at pH = 2; 99 at pH = 7)

2.3 9.8 -- 131.18 1.09 1.67 0.47

Methionine Met M Hydroxyl or Sulfur-Containing, nonpolar Very Hydrophobic (74 at pH = 2; 74 at pH = 7)

2.1 9.3 -- 149.21 1.30 1.14 0.52

Serine Ser S Hydroxyl or Sulfur-Containing, polar Neutral (-7 at pH = 2; -5 at pH = 7)

2.2 9.2 -- 105.09 0.57 0.96 1.22

Cysteine Cys C Hydroxyl or Sulfur-Containing, polar Hydrophobic (52 at pH = 2; 49 at pH = 7)

1.9 10.7 8.4 121.16 0.66 2.40 0.54

Threonine Thr T Hydroxyl or Sulfur-Containing, polar Neutral (13 at pH = 2; 13 at pH = 7)

2.1 9.1 -- 119.12 0.76 1.17 0.96

Proline Pro P Cyclic Hydrophilic (-46 at pH = 2; -46 at pH = 7)

2.0 9.6 -- 115.13 0.34 0.31 1.32

Phenylalanine Phe F Aromatic Very Hydrophobic (92 at pH = 2; 100 at pH = 7)

2.2 9.3 -- 165.19 1.16 1.33 0.59

Tyrosine Tyr Y Aromatic Hydrophobic (49 at pH = 2; 63 at pH = 7)

2.2 9.2 10.5 181.19 0.74 1.45 0.76

Tryptophan Trp W Aromatic Very Hydrophobic (84 at pH = 2; 97 at pH = 7)

2.5 9.4 -- 204.25 1.02 1.35 0.65

Histidine His H Basic Hydrophilic at pH=2 (-42), Neutral at pH=7 (8)

1.8 9.3 6.0 155.16 1.05 0.80 0.81

Lysine Lys K Basic Hydrophilic (-37 at pH = 2; -23 at pH = 7)

2.2 9.1 10.5 146.188 1.23 0.69 1.07

Arginine Arg R Basic Hydrophilic (-26 at pH = 2; -14 at pH = 7)

1.8 9.0 12.5 174.2 1.21 0.84 0.90

Aspartate Asp D Acidic Neutral at pH=2 (-18), Hydrophilic at pH=7 (-55)

2.0 9.9 3.9 133.10 0.99 0.39 1.24

Glutamate Glu E Acidic Neutral at ph=2 (8), Hydrophilic at pH=7 (-31)

2.1 9.5 4.1 147.13 1.59 0.52 1.01

Asparagine Asn N Acidic, polar Hydrophilic (-41 at pH = 2; -28 at pH = 7)

2.1 8.7 -- 132.118 0.76 0.48 1.34

Glutamine Gln

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