Essential for humans. Phenylalanine, tyrosine, and tryptophan contain large rigid aromatic group on the side chain. These are the biggest amino acids. Like isoleucine, leucine and valine, these are hydrophobic and tend to orient towards the interior of the folded protein molecule.
Because of the two hydrogen atoms at the ? carbon, glycine is not optically active. It is the tiniest amino acid, rotates easily, adds flexibility to the protein chain. It is able to fit into the tightest spaces, e.g., the triple helix of collagen. As too much flexibility is usually not desired, as a structural component it is less common than alanine.
In even slightly acidic conditions protonation of the nitrogen occurs, changing the properties of histidine and the polypeptide as a whole. It is used by many proteins as a regulatory mechanism, changing the conformation and behavior of the polypeptide in acidic regions such as the late endosome or lysosome, enforcing conformation change in enzymes. However only a few histidines are needed for this, so it is comparatively scarce.
I
Ile
ไอโซลูซีน (Isoleucine)
ไฮโดรโฟบิก
131.17
6.05
2.32
9.76
Essential for humans. Isoleucine, leucine and valine have large aliphatic hydrophobic side chains. Their molecules are rigid, and their mutual hydrophobic interactions are important for the correct folding of proteins, as these chains tend to be located inside of the protein molecule.
Essential for humans. Behaves similarly to arginine. Contains a long flexible side-chain with a positively-charged end. The flexibility of the chain makes lysine and arginine suitable for binding to molecules with many negative charges on their surfaces. E.g., DNA-binding proteins have their active regions rich with arginine and lysine. The strong charge makes these two amino acids prone to be located on the outer hydrophilic surfaces of the proteins; when they are found inside, they are usually paired with a corresponding negatively-charged amino acid, e.g., aspartate or glutamate.
Essential for humans. Always the first amino acid to be incorporated into a protein; sometimes removed after translation. Like cysteine, contains sulfur, but with a methyl group instead of hydrogen. This methyl group can be activated, and is used in many reactions where a new carbon atom is being added to another molecule.
Contains an unusual ring to the N-end amine group, which forces the CO-NH amide sequence into a fixed conformation. Can disrupt protein folding structures like ? helix or ? sheet, forcing the desired kink in the protein chain. Common in collagen, where it undergoes a posttranslational modification to hydroxyproline. Uncommon elsewhere.
Q
Gln
กลูตามีน (Glutamine)
ไฮโดรฟิลิก
146.15
5.65
2.17
9.13
Neutralized version of glutamic acid. Used in proteins and as a storage for ammonia.
Serine and threonine have a short group ended with a hydroxyl group. Its hydrogen is easy to remove, so serine and threonine often act as hydrogen donors in enzymes. Both are very hydrophylic, therefore the outer regions of soluble proteins tend to be rich with them.
รายช, อกรดอะม, โนมาตรฐาน, list, standard, amino, acids, แสดงโดยศ, ตรโครงสร, าง, structures, ตรโครงสร, างและส, ญญล, กษณ, และรห, สพ, นธ, กรรม, genetic, code, ของ, กรดอะม, โน, วเป, นด, งน, แสดงรายช, อกรดอะม, โนและค, ณสมบ, ทางเคม, chemical, properties, แสดงเป, นตา. raychuxkrdxamionmatrthan List of standard amino acids aesdngodysutrokhrngsrang Structures sutrokhrngsrangaelasyylksnaelarhsphnthukrrm genetic code khxng krdxamion 20 twepndngni aesdngraychuxkrdxamionaelakhunsmbtithangekhmi Chemical properties aesdngepntarangthimithngsyylksn 1 twxksr aela 3 twxksr aelakhunsmbtithangekhmi sungaetktangkniptam oskhang side chains nahnkomelkul sungepnkhaechliykhxngixosothpthnghmdrwmthngnahnkkhxngnadwy H2O Abbrev chuxetm Full Name praephthoskhang Side chain type mwl Mass pI Isoelectric point pK1 COOH pK2 NH3 pKr R RemarksA Ala xalanin Alanine ihodrofbik hydrophobic 89 09 6 01 2 35 9 87 micanwnmakmay mipraoychnhlayxyang mikhwamaekhngmakkwaiklsin aetmikhnadelkphxthicacdwangintaaehnngthiehmaasmsahrbokhrngsrangkhxngoprtin mnkhxnkhangwangtwepnklangsamarthxyuidthngekhtthiepn ihodrfilik bnoprtinswnnxk aelabriewnthiepnihodrofbikphayinC Cys sisethxin Cysteine ihodrofbik Nagano 1999 121 16 5 05 1 92 10 70 8 37 xatxmkhxngkamathnechuxmtxkbixxxnkhxng olhahnk phayitphawaxxksiidsing sistixin 2 omelkulsamarthechuxmtxsungknaelaknidodn phnthaidslifd disulfide bond aelaekidepnkrdxamion sistin emuxsistinepnswnhnungkhxngoprtin xinsulin mncamiaerngthithaihokhrngsrangkhxng xinsulin epnaebb ethxrethiyri strkecxr aelathaihoprtinthntxkarphbngxaela phidthrrmchati karechuxmtxaebbidslifd disulphide bridges phbidepnsingthrrmdainoprtinsungcatxngthahnathiinsingaewdlxmthirunaerng exnismyxyxahar echn eppsin aela ikhomthripsin oprtinokhrngsrang structural proteins echn ekhxratin aela oprtinthielkekinipthicakhngrupkhxngmniw echn xinsulin D Asp krdaexspartik Aspartic acid epnkrd 133 10 2 85 1 99 9 90 3 90 cathangankhlaykbkrdklutamik epnklumthiepnkrdihodrfilikmipraculbthiaekhngaekrng mkcatngxyubnphunphiwdannxkkhxngoprtinthaihlalaynaid cbkbpracubwkkhxngomelkulaelaixxxn mkxyurwmkbexnisminkarcbkbixxxnolha emuxxyudaninkhxngoprtin aspartate aela glutamate camikarcbkhukbxarciniaelailsinE Glu krdklutamik Glutamic acid epnkrd 147 13 3 15 2 10 9 47 4 07 cathangankhlaykbkrd aspartic miphnthayawkwaaelabangkwa mikhwamyudhyunmakkwaF Phe finilxalanin Phenylalanine ihodrofbik 165 19 5 49 2 20 9 31 Essential for humans Phenylalanine tyrosine and tryptophan contain large rigid aromatic group on the side chain These are the biggest amino acids Like isoleucine leucine and valine these are hydrophobic and tend to orient towards the interior of the folded protein molecule G Gly iklsin Glycine ihodrfilik 75 07 6 06 2 35 9 78 Because of the two hydrogen atoms at the carbon glycine is not optically active It is the tiniest amino acid rotates easily adds flexibility to the protein chain It is able to fit into the tightest spaces e g the triple helix of collagen As too much flexibility is usually not desired as a structural component it is less common than alanine H His histidin Histidine epnebs 155 16 7 60 1 80 9 33 6 04 In even slightly acidic conditions protonation of the nitrogen occurs changing the properties of histidine and the polypeptide as a whole It is used by many proteins as a regulatory mechanism changing the conformation and behavior of the polypeptide in acidic regions such as the late endosome or lysosome enforcing conformation change in enzymes However only a few histidines are needed for this so it is comparatively scarce I Ile ixoslusin Isoleucine ihodrofbik 131 17 6 05 2 32 9 76 Essential for humans Isoleucine leucine and valine have large aliphatic hydrophobic side chains Their molecules are rigid and their mutual hydrophobic interactions are important for the correct folding of proteins as these chains tend to be located inside of the protein molecule K Lys ilsin Lysine epnebs 146 19 9 60 2 16 9 06 10 54 Essential for humans Behaves similarly to arginine Contains a long flexible side chain with a positively charged end The flexibility of the chain makes lysine and arginine suitable for binding to molecules with many negative charges on their surfaces E g DNA binding proteins have their active regions rich with arginine and lysine The strong charge makes these two amino acids prone to be located on the outer hydrophilic surfaces of the proteins when they are found inside they are usually paired with a corresponding negatively charged amino acid e g aspartate or glutamate L Leu liwsin Leucine ihodrofbik 131 17 6 01 2 33 9 74 Essential for humans Behaves similar to isoleucine and valine See isoleucine M Met emithoxnin Methionine ihodrofbik 149 21 5 74 2 13 9 28 Essential for humans Always the first amino acid to be incorporated into a protein sometimes removed after translation Like cysteine contains sulfur but with a methyl group instead of hydrogen This methyl group can be activated and is used in many reactions where a new carbon atom is being added to another molecule N Asn aexspharacin Asparagine ihodrfilik 132 12 5 41 2 14 8 72 Neutralized version of aspartic acid P Pro oprlin Proline ihodrofbik 115 13 6 30 1 95 10 64 Contains an unusual ring to the N end amine group which forces the CO NH amide sequence into a fixed conformation Can disrupt protein folding structures like helix or sheet forcing the desired kink in the protein chain Common in collagen where it undergoes a posttranslational modification to hydroxyproline Uncommon elsewhere Q Gln klutamin Glutamine ihodrfilik 146 15 5 65 2 17 9 13 Neutralized version of glutamic acid Used in proteins and as a storage for ammonia R Arg Arginine epnebs 174 20 10 76 1 82 8 99 12 48 Functionally similar to lysine S Ser esxrin Serine ihodrofbik 105 09 5 68 2 19 9 21 Serine and threonine have a short group ended with a hydroxyl group Its hydrogen is easy to remove so serine and threonine often act as hydrogen donors in enzymes Both are very hydrophylic therefore the outer regions of soluble proteins tend to be rich with them T Thr thrioxnin Threonine ihodrfilik 119 12 5 60 2 09 9 10 Essential for humans Behaves similarly to serine V Val warin Valine ihodrofbik 117 15 6 00 2 39 9 74 Essential for humans Behaves similarly to isoleucine and leucine See isoleucine W Trp thripotaefn Tryptophan ihodrofbik 204 23 5 89 2 46 9 41 Essential for humans Behaves similarly to phenylalanine and tyrosine see phenylalanine Precursor of serotonin Y Tyr ithorsin Tyrosine ihodrofbik 181 19 5 64 2 20 9 21 10 46 Behaves similarly to phenylalanine and tryptophan see phenylalanine Precursor of melanin epinephrine and thyroid hormones Amino acid Abbrev Side chain Hydro phobic Polar Charged Small Tiny Aromatic or Aliphatic van der Waals volume Codon Occurrence in proteins Alanine Ala A CH3 X X X 67 GCU GCC GCA GCG 7 8Cysteine Cys C CH2SH X X 86 UGU UGC 1 9Aspartate Asp D CH2COOH X negative X 91 GAU GAC 5 3Glutamate Glu E CH2CH2COOH X negative 109 GAA GAG 6 3Phenylalanine Phe F CH2C6H5 X Aromatic 135 UUU UUC 3 9Glycine Gly G H X X X 48 GGU GGC GGA GGG 7 2Histidine His H CH2 C3H3N2 X positive Aromatic 118 CAU CAC 2 3Isoleucine Ile I CH CH3 CH2CH3 X Aliphatic 124 AUU AUC AUA 5 3Lysine Lys K CH2 4NH2 X positive 135 AAA AAG 5 9Leucine Leu L CH2CH CH3 2 X Aliphatic 124 UUA UUG CUU CUC CUA CUG 9 1Methionine Met M CH2CH2SCH3 X 124 AUG 2 3Asparagine Asn N CH2CONH2 X X 96 AAU AAC 4 3Proline Pro P CH2CH2CH2 X X 90 CCU CCC CCA CCG 5 2Glutamine Gln Q CH2CH2CONH2 X 114 CAA CAG 4 2Arginine Arg R CH2 3NH C NH NH2 X positive 148 CGU CGC CGA CGG AGA AGG 5 1Serine Ser S CH2OH X X X 73 UCU UCC UCA UCG AGU AGC 6 8Threonine Thr T CH OH CH3 X X X 93 ACU ACC ACA ACG 5 9Valine Val V CH CH3 2 X X Aliphatic 105 GUU GUC GUA GUG 6 6Tryptophan Trp W CH2C8H5N X Aromatic 163 UGG 1 4Tyrosine Tyr Y CH2 C6H4OH X X Aromatic 141 UAU UAC 3 2duephim aekikhkrdxamion bthkhwamekiywkbchiwekhmi ekhmixinthriy aelaomelkulchiwphaphniyngepnokhrng khunsamarthchwywikiphiediyidodyephimkhxmulekhathungcak https th wikipedia org w index php title raychuxkrdxamionmatrthan amp oldid 9495838, wikipedia, วิกิ หนังสือ, หนังสือ, ห้องสมุด,
