Protein Secondary Structure Lecture 2192003 Three Dimensional Protein
- Slides: 13
Protein Secondary Structure Lecture 2/19/2003
Three Dimensional Protein Structures Confirmation: Spatial arrangement of atoms that depend on bonds and bond rotations. Proteins can change conformation, however, most proteins have a stable “native” conformation. The native protein is folded through weak interactions: a) hydrophobic interaction b) Hydrogen bonds c) Ionic bonds d) Van der Waals attractions
A Denatured protein is unfolded, random dangling, and often precipitated (cooking egg whites). The Native conformation is dictated by its amino acid sequence. primary structure is everything. A one dimensional strand of DNA contains four dimensional data: height width depth life span!!
The Amide bond Linus Pauling and Corey determined the structure of the peptide bond by X-ray. 40% double bond character. The amide bond or peptide bond C-N bond is 0. 13 A shorter than C -N bond. The carbonyl bond is. 02 A longer then those for ketones and aldehydes Resonance gives 85 k. J • mole-1 stability when bond is planar!!
Peptide bonds are planar Resonance energy depends on bond angle: 180 is max angle cis or trans peptide bond. Most peptide bonds are trans, 10% that follow proline may be cis Note: differences between bond angles and bond lengths comparing cis and trans forms.
Torsion angles Rotation or dihedral angles C -N C -C phi psi When a peptide chain is fully extended the angles are defined as 180 or -180. At 180 one gets a staggered conformation. (all trans) i. e. ethane Note: alternating C=O pointing in opposite directions.
When viewed down the N to C terminus axis, rotation to the right or clock wise increases the angle of rotation. Must start with the fully extended form which is defined as 180 o or -180 o Note: this picture and the one in the book is not correct!! The Y angle should go the other direction
Start with fully extended protein structure Rotate counter clockwise start at +180 o and decrease angle Rotate clockwise start at -180 o and increase angle This is C -carbonyl bond or psi angle, Y
Ethane can exist as staggered or eclipsed conformation Staggered eclipsed There is a 12 k. J • mole-1 penalty in energy for an eclipsed geometry Bulky amino acid side chains have a much higher energy penalty. There a few favored geometries which the protein backbone can fold
If all + angles are defined then the backbone structure of a protein will be known!! These angles allow a method to describe the protein’s structure and all backbone atoms can be placed in a 3 d grid with an x, y, z coordinate.
Ramachandran plot If you plot on the y axis and on the x axis, you will plot all possible combinations of , . This plot shows which angles are allowed or which angles are sterically hindered for poly-l-alanine
Secondary structure can be defined by f and angles F Y -57 -47 sheet -119 113 sheet -139 135 310 helix -49 -26 collagen -51 153 helix rt handed Repeating local protein structure determined by hydrogen bonding 12 proteins except for Gly and Pro helices and pleated sheets.
Steric hindrance between the amide nitrogen and the carbonyl F = -60 o and Y = 30 o
- Circular motion is one dimensional or two dimensional
- Alpha helix and beta sheet
- Super secondary structure of protein
- Primary level of protein structure
- Primary secondary and tertiary protein structure
- Protein primary structure
- Primary secondary and tertiary protein structure
- Beta meander motif
- Super secondary structure of protein
- Expasy
- Nnuuu
- Primary secondary and tertiary structure of protein
- 01:640:244 lecture notes - lecture 15: plat, idah, farad
- What are two and three dimensional shapes