Seven - Myoglobin & Hemoglobin

Seven - Myoglobin & Hemoglobin - Myoglobin has...

Info iconThis preview shows page 1. Sign up to view the full content.

View Full Document Right Arrow Icon
Illustrates important concepts a) b) importance of noncovalent interactions i. reversible binding of a ligang to a protein c) buffering capacity Hemoglobin functions as a buffer in blood The better the crystal the better the resolution the better the defraction pattern. Myoglobin stores oxygen in muscle and only release under extreme conditions
Background image of page 1
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: Myoglobin has tertiary structure Hemoglobin is quaternary structure In addition to oxygen, hemoglobin bind to carbon dioxide and H+ This helps with buffering capacity Heme = very planar and very hydrophobic Oxygen bonding causes disruption in noncovalent interactions...
View Full Document

This note was uploaded on 03/19/2012 for the course BIO 2000 taught by Professor Ewr during the Spring '12 term at Alabama.

Ask a homework question - tutors are online