Chapter1 Protein课件.ppt

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Chapter1 Protein课件

Chapter 1 Protein Contents Chemical components Molecular structures Structure-function relationship Physical and chemical properties What are proteins? Proteins are macromolecules composed of amino acids linked together through peptide bonds. How are about proteins? the most widely distributed biomolecules the most abundant biomolecules (45% of human body) the most complex biomolecules the most diversified biological functions What do proteins do? Components of proteins major elements C (50~55%), H (~7%), O (19~20%), N (13~19%), S (~4%) trace elements P, Fe, Cu, Zn, I, … The average nitrogen content in proteins is about 16%, and proteins are the major source of N in biological systems. The protein quantity can be estimated. protein in 100g sample = N per gram x 6.25 x 100 §1.1 Amino Acids The basic building blocks of proteins About 300 types of AAs in nature, but only 20 types are used for protein synthesis in biological systems. A amino group, a carboxyl group, a H atom and a R group are connected to a C atom. The C atom is an optically active center. L-Amino acid §1.1.a Classification The R groups, also called side chains, make each AA unique and distinctive. Aas are grouped as (1) non-polar, hydrophobic; (2) polar, neutral; (3) basic; (4) acidic. Non-polar and hydrophobic AAs R groups are non-polar, hydrophobic aliphatic or aromatic groups. R groups are uncharged. AAs are insoluble in H2O. Polar and uncharged AAs R groups are polar: -OH, -SH, and -NH2. R groups are highly reactive. AAs are soluble in H2O, that is, hydrophilic. Basic AAs R groups have one -NH2. R groups are positively charged at neutral pH (=7.0). AAs are highly hydrophilic. Acidic AAs R groups have –COOH. R groups are negatively charged at physiological pH (=7.4). AAs are soluble in H2O. Special amino acids - Gly optically inactive Special amino acids - Pro Having a ring structure and imino group Special amino acids - Cys §1.

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