Lectures: 2,009 | Views: 38,199,216 | Subscribers: 287,239 | Subscribe
Basic and Acidic Amino Acids
The remaining five amino acids are highly hydrophobic and polar. This is because they have a full charge on their side chain group at the normal physiological pH. Lysine and arginine are basic amino acids because their side chain group contains a full positive charge at the physiological pH. Histidine is also considered basic but it can have a positive or a neutral charge on its side chain group at the physiological pH. This is because histidine's side chain has a pKa value of 6.0. Aspartate and glutamate are the two acidic amino acids, which means that they both have a full negative charge on their side chains at the normal physiological pH. When aspartate and glutamate are exposed to a very low pH, their carboxylate ion group will be protonated, thereby turning them into aspartic acid and glutamic acid, respectively.
[{"id":"ZfsuDfui0oU","title":"Introduction to Proteins","link":"http:\/\/www.aklectures.com\/lecture\/introduction-to-proteins"},{"id":"LHNNOIMt5x0","title":"Introduction to Amino Acids","link":"http:\/\/www.aklectures.com\/lecture\/introduction-to-amino-acids"},{"id":"cL2_e83v3js","title":"Nonpolar and Uncharged Polar Amino Acids","link":"http:\/\/www.aklectures.com\/lecture\/nonpolar-and-uncharged-polar-amino-acids"},{"id":"dF48PWHbA10","title":"Basic and Acidic Amino Acids","link":"http:\/\/www.aklectures.com\/lecture\/basic-and-acidic-amino-acids"},{"id":"eE4WgONS6-k","title":"Ionizable Amino Acids","link":"http:\/\/www.aklectures.com\/lecture\/ionizable-amino-acids"},{"id":"4_2fA_W7snM","title":"Peptide Bond Formation","link":"http:\/\/www.aklectures.com\/lecture\/peptide-bond-formation"},{"id":"KW8Uo8jsiGY","title":"Primary Structure of Proteins","link":"http:\/\/www.aklectures.com\/lecture\/primary-structure-of-proteins"},{"id":"qNWZCIoldWA","title":"Primary Structure of Proteins (Part II)","link":"http:\/\/www.aklectures.com\/lecture\/primary-structure-of-proteins-part-ii"},{"id":"4YbwjjZWGPA","title":"Secondary Structure of Proteins","link":"http:\/\/www.aklectures.com\/lecture\/secondary-structure-of-proteins"},{"id":"p5Oi_yFfAhg","title":"Tertiary Structure of Proteins","link":"http:\/\/www.aklectures.com\/lecture\/tertiary-structure-of-proteins"},{"id":"-3uYmi7C2DI","title":"Quaternary Structure of Proteins","link":"http:\/\/www.aklectures.com\/lecture\/quaternary-structure-of-proteins"},{"id":"pZee0XCCqH4","title":"Anfinsen's Experiment of Protein Folding","link":"http:\/\/www.aklectures.com\/lecture\/anfinsens-experiment-of-protein-folding"},{"id":"Chs7ixRstQk","title":"Prions and Protein Misfolding","link":"http:\/\/www.aklectures.com\/lecture\/prions-and-protein-misfolding"},{"id":"9XK1Ekx5tYc","title":"Cooperativity of Protein Folding","link":"http:\/\/www.aklectures.com\/lecture\/cooperativity-of-protein-folding"},{"id":"gpnyMM44lXc","title":"Modification of Amino Acids","link":"http:\/\/www.aklectures.com\/lecture\/modification-of-amino-acids"}]
Comments
Playlists
Login to create and share playlists