IUB BIOL-L 112 - Proteins and Amino Acids (2 pages)

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Proteins and Amino Acids



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Proteins and Amino Acids

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Lecture number:
5
Pages:
2
Type:
Lecture Note
School:
Indiana University, Bloomington
Course:
Biol-L 112 - Foundations of Biology: Biological Mechanisms

Unformatted text preview:

BIOL L 112 1nd Edition Lecture 5 Outline of Last Lecture I Polymers II Carbohydrates A Monosaccharides B Disaccharides C Polysaccharides i Glycogen ii Starch iii Cellulose III Lipids A Fats i Saturated Fat ii Unsaturated Fat iii Trans Fat B Phospholipids C Steroids Outline of Current Lecture I Proteins II Amino Acids A Nonpolar Side Chains B Polar Side Chains C Electrically Charged Side Chains Current Lecture I Proteins are defined as one or more polypeptides which is a polymer of amino acids Each polypeptide is folded into a specific and unique 3D shape that determines function They have many different structures and functions II Amino acids are monomers that are covalently linked together through peptide bonds to make polypeptides These peptide bonds are formed through dehydration reactions Amino acids are made of an asymmetric carbon that is attached to an amino group a carboxyl group and a side chain R group The amino and carboxyl groups are usually in their ionized forms at the pH of a cell Amino acids are categorized into polar nonpolar or electrically charged by looking at their side chains These notes represent a detailed interpretation of the professor s lecture GradeBuddy is best used as a supplement to your own notes not as a substitute A Nonpolar side chains are hydrophobic because they are made of hydrocarbons When they are bonded they form hydrophobic interactions B Polar side chains are hydrophilic and are able to form hydrogen bonds C Electrically charged side chains are hydrophilic and are able to form ionic and hydrogen bonds They can be acidic or basic depending on if they are negatively or positively charged



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