Biology Lecture 7 - polypeptide. Also play a role in the 3D...

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Biology Lecture 7 Amino acids join together to form polypeptides Proteins account for more than 50% of the dry mass of most cells Important proteins to know now include: Enzymatic proteins Structural proteins Storage proteins Proteins for later in the semester: Transport proteins Motor proteins Enzymes are proteins that act as catalyst (speed up reaction but aren’t consumed by it) Most structurally sophisticated molecules Polypeptides are in linear arrangement. They are built from the same 20 sets of amino acids. Proteins are made from one or several polypeptides The groove is the space where an enzyme is going to connect with its partner. Amino acids are organic molecules Contain an alpha carbon, hydrogen atom, carboxyl group, amino group, and a differing side chain called R R group determines how the amino acid interacts with other amino acids within the
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Unformatted text preview: polypeptide. Also play a role in the 3D structure that it takes on The 4 R groups are non-polar, polar, acidic, and basic Non-polar amino acids tend to contain methyal in their R group and are hydrophobic Polar amino acids tend to contain hydroxyl in their R group and they are hydrophilic Acidic R group is donating hydrogen atoms. They have a negative charge. Basic R group is receiving hydrogen atoms. They have a positive charge. Amino acids are linked by peptide bonds to form polypeptides. Formed by dehydration reactions Each polypeptide has a unique linear sequence Proteins twists and folds into a unique shapes based on the R groups interacting with each other. The chains tend to fold spontaneously into shape The proteins function depends on the binding to another molecule Look at figure 2.18 in the textbook...
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This note was uploaded on 05/03/2011 for the course BIO 311 C taught by Professor Mcclelland during the Fall '09 term at University of Texas at Austin.

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