DOC PREVIEW
U-M BIOLCHEM 415 - Protein Structure and Folding
Type Lecture Note
Pages 3

This preview shows page 1 out of 3 pages.

Save
View full document
View full document
Premium Document
Do you want full access? Go Premium and unlock all 3 pages.
Access to all documents
Download any document
Ad free experience
Premium Document
Do you want full access? Go Premium and unlock all 3 pages.
Access to all documents
Download any document
Ad free experience

Unformatted text preview:

BIOLCHEM 415 1st Edition Lecture 4 Outline of Last Lecture I. Proteins are linear polymers made of 20 different amino acidsII. Amino Acids have different functional propertiesIII. Protein structure: primary, secondary, tertiary, and quaternaryIV. Primary structure: the sequence of amino acidsOutline of Current Lecture V. Hierarchial Protein Structure: primary, secondary, tertiary, quaternaryVI. Secondary structures: α-helices and β-sheetsVII. Protein folding is driven by the hydrophobic effectVIII. Disulfide bonds stabilize protein structureIX. Protein misfolding can contribute to diseasesCurrent LectureSecondary Structure- the Alpha (α) helix- 3.6 residues/turn and 5.4Å/turn- carbonyl and amide groups of peptide bonds are hydrogen bonded- h-bonds between i and i+4 residues- right-handed helix- side chains face outwards- the β sheetThese notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.- each unit is a β-strand- interact with other strands in parallel and antiparallel orientations- C=O h-bonds to N-H in adjacent strands- twisted shape- mixed sheets have both parallel and antiparallel orientationsTertiary Structure- how the secondary elements relate to each other- Myoglobin- completely comprised of α-helices- Fatty acid bonding protein- β-strands (form a β-barrel structure)- some α-helicesDomain- a discrete region in polypeptide chain that folds into an independent unit- usually globular (100-400 amino acids)Quaternary structure- 2 or more polypeptide chains - Cro-protein- dimer with 2 polypeptides- Hemoglobin - tetramer of 2 α subunits and 2 β subunitsProtein Folding- new proteins are unfolded with many different conformations- folded adopt single uniform conformation- powered by hydrophobic effect- hydrophobic amino acids buried in interior of protein- shielded from water- hydrophilic and charged found on the surface (h-bonds)- hydrophobic amino acids inside use van der waalsThermodynamics of Protein Folding- represented by funnel- top = unfolded all possible conformations- molten globule = intermediate- bottom = folded with lowest energyRibonuclease A- disulfide bonds (hydrogen pairs)- not readily denatured- disulfide bonds must be reduced first (denaturate)β-mercaptoethanol- reduces disulfide bonds- new disulfide bonds formed in itselfDiseases caused by protein misfolding- Baline Spongiform Encephalitis and Creutzfeldt-Jacob- prion protein aggregation in neural tissue- death of neurons- formation of amyloid fibers and plaques from neuronal protons - Alzheimer’s and Parkinson’s - neuron


View Full Document

U-M BIOLCHEM 415 - Protein Structure and Folding

Type: Lecture Note
Pages: 3
Documents in this Course
Load more
Download Protein Structure and Folding
Our administrator received your request to download this document. We will send you the file to your email shortly.
Loading Unlocking...
Login

Join to view Protein Structure and Folding and access 3M+ class-specific study document.

or
We will never post anything without your permission.
Don't have an account?
Sign Up

Join to view Protein Structure and Folding 2 2 and access 3M+ class-specific study document.

or

By creating an account you agree to our Privacy Policy and Terms Of Use

Already a member?