Lecture7 - Lecture 7 1/21/09 Background reading: Garrett...

Info iconThis preview shows pages 1–3. Sign up to view the full content.

View Full Document Right Arrow Icon
Lecture 7 1/21/09 Outline: Amino acid sequencing Functional diversity of proteins Primary structure of proteins (I o Structure) Secondary structure of proteins (II o Structure) X-ray crystallography α helix Random coil β sheet Background reading: Garrett and Grisham: Chapter 6: Pages 153 - 165
Background image of page 1

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

View Full DocumentRight Arrow Icon
Amino acid sequencing 1) Determine amino acid composition 2) Determine amino acid present at each end of the peptide. 3) Determine sequence of amino acids in between each end. Strategy: Fragment to smaller peptides by various methods and hope to obtain overlapping fragments and put together. Functional diversity of proteins Proteins are most abundant organic molecules in cells and account for >50% of dry weight of cell. Great functional diversity. Examples: Hormones Enzymes Antibodies Transport Contractile systems Structural proteins All proteins composed of same set of about 20 amino acids, which by themselves have no activity. The conformation of the peptide or protein is important since it allows their reactive groups to be at the right spatial positions to interact with themselves or other molecules.
Background image of page 2
Image of page 3
This is the end of the preview. Sign up to access the rest of the document.

This note was uploaded on 02/21/2009 for the course BIS BIS102 taught by Professor Hilt during the Winter '08 term at UC Davis.

Page1 / 11

Lecture7 - Lecture 7 1/21/09 Background reading: Garrett...

This preview shows document pages 1 - 3. Sign up to view the full document.

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