CHEM 1000 Lecture Notes - Lecture 22: Zwitterion, Protein Folding, Carboxylic Acid

70 views3 pages
28 Nov 2017
School
Department
Course
Professor

Document Summary

Proteins large biomolecules consisting of long chains of amino acid residues. Amino acids contain both an amine and a carboxylate group attached to the same carbon (20 different amino acids) Dipeptide formed when 2 amino acids are joined. Proteins may contain 10,000+ amino acids units. Zwitterion a compound in which the negative charge and positive charge are on the different parts of the same molecule. Amino acids tend to exist as a dipolar ion or zwitterion at physiological ph. Peptide sequences sequence of the amino acids in a protein is critical. Written from the free amino group (n-terminal) to the free carboxyl group (c- terminal) Primary structure sequence of amino acids from n-terminal to c-terminal. Secondary structure way the polypeptide chain folds or coils as a result of hydrogen bonding of the backbone amide groups. Tertiary structure 3-d shape of a protein are relatively far apart in the protein chain. Protein folding creates spatial relationships between amino-acid units that.

Get access

Grade+20% off
$8 USD/m$10 USD/m
Billed $96 USD annually
Grade+
Homework Help
Study Guides
Textbook Solutions
Class Notes
Textbook Notes
Booster Class
40 Verified Answers
Class+
$8 USD/m
Billed $96 USD annually
Class+
Homework Help
Study Guides
Textbook Solutions
Class Notes
Textbook Notes
Booster Class
30 Verified Answers

Related textbook solutions

Related Documents

Related Questions