BCH110A-LEC3-4_AminoAcids-Peptides_11

BCH110A-LEC3-4_AminoAcids-Peptides_11 - BCH 110A, Fall 2011...

Info iconThis preview shows pages 1–4. Sign up to view the full content.

View Full Document Right Arrow Icon
BCH 110A, Fall 2011 Lec 3-4, Amino Acids and Protein Primary Structure (Dr. Baldwin © 2011) 1 Lectures 3-4 Introduction to Proteins: Amino Acids, the Building Blocks of Proteins; Peptide Bonds You should KNOW the structures of all 20 amino acids by beginning of Lecture 3 (Wed. 9/28/11). Reading : Lehninger Principles , 5th ed.: chapt. 3, pp. 71-85; 92-94; 102-107; chapt. 4 (pp. 115-117) See also posted General Chemistry Review notes for acid-base concepts, and online website on amino acids (below) for excellent way to learn the amino acids’ structures and properties: http://www.biology.arizona.edu/biochemistry/problem_sets/aa/aa.html Lecture may skip portions of these notes and use website, or go back and forth. BIOCHEMISTRY 110A Fall 2011 T. Baldwin "Once we realize that imperfect understanding is the human condition, there is no shame in being wrong, only in failing to correct our mistakes." - George Soros (1912-1994) Romanian-French dramatist "Soros on Soros" "Human beings, who are almost unique in having the ability to learn from the experience of others, are also remarkable for their apparent disinclination to do so." - Douglas Adams (1952-) English novelist
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
BCH 110A, Fall 2011 Lec 3-4, Amino Acids and Protein Primary Structure (Dr. Baldwin © 2011) 2 Key Concepts 4 levels of protein structure Primary (1°) Secondary (2°) Tertiary (3°) Quaternary (4°) Properties of the 20 amino acids that occur in peptides and proteins are crucial to the structure and function of proteins. – Stereochemistry – Relative hydrophobicity or polarity – Hydrogen bonding properties – Ionization properties – Other chemical properties, e.g., nucleophilicity linked functions : how 2 ligands affect each other’s binding affinity by the same factor (cysteine deprotonation reactions as an example) Proteins: primary structure Peptide bond • amide linkage holding amino acid residues in peptide and protein polymers (primary structure of proteins). • Product of condensation of 2 amino acids Key Concepts, continued Proteins: primary structure Peptide bond • amide linkage holding amino acid residues in peptide and protein polymers (primary structure of proteins). • Product of condensation of 2 amino acids Posttranslational modifications of amino acids/proteins Examples: • hydroxylation of some Pro and Lys residues in collagen (vital for collagen structure) • carboxylation of some Glu residues (vital for blood clotting) • reversible phosphorylation of some Ser, Thr, and Tyr residues (vital for many regulatory processes) • proteolytic cleavage (vital for some regulatory processes and in digestion of protein nutrients) • disulfide bond formation (vital for structures of some proteins, especially extracellular proteins, and in some coenzyme and enzyme activities) Sequence of amino acids in protein (primary structure) determines 3-dimensional folding pattern of protein (higher levels of structure).
Background image of page 2
BCH 110A, Fall 2011 Lec 3-4, Amino Acids and Protein Primary Structure (Dr. Baldwin © 2011) 3 Learning Objectives
Background image of page 3

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Image of page 4
This is the end of the preview. Sign up to access the rest of the document.

This document was uploaded on 10/26/2011 for the course BCH 110a at UC Riverside.

Page1 / 32

BCH110A-LEC3-4_AminoAcids-Peptides_11 - BCH 110A, Fall 2011...

This preview shows document pages 1 - 4. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online