Topic 4, protein folding.ppt.edu

Topic 4, protein folding.ppt.edu - Topic 4Protein Folding...

Info iconThis preview shows pages 1–10. Sign up to view the full content.

View Full Document Right Arrow Icon

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

View Full DocumentRight Arrow Icon

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

View Full DocumentRight Arrow Icon

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

View Full DocumentRight Arrow Icon

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

View Full DocumentRight Arrow Icon

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

View Full DocumentRight Arrow Icon
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: Topic 4Protein Folding How do you get this from that? Learning Objectives Be able to define the following terms: protein folding, alpha-helix, beta-sheet, loop, disulfide bond Be able to explain why protein structure is critical to protein function Understand the order of protein structure and how each level contributes to the final structure Primary, secondary, tertiary, quaternary Be able to classify peptide or protein structures to the proper class (e.g., alpha- What do proteins do? Proteins make things: synthesize DNA, RNA, and other proteins Proteins destroy things: recycling of old cellular materials, pathogen destruction, etc. Proteins are a major component for communication both within a single cell and between different cells, both near and far Proteins do nearly everything for you except for encoding the genetic material Why is protein structure important? Proteins have a particular structure so that they can interact with different things (e.g., other proteins, DNA, RNA, small molecules) If a protein doesnt fold into the proper structure, it cannot carry out intended function Protein folding to the correct conformation is often spontaneous As a protein exists the ribosome, it will naturally begin to form secondary and tertiary structures Chaperone proteins can assist in the process by detecting improper folding, and assisting in re-folding Proteins (chains of amino acids) can only function properly if in the correct shape. Many proteins are activated or de-activated by changing of shape. How do proteins develop the correct shape if they are produced in a linear form? --This is the topic for today =just the primary sequence of a chain of amino acids Structures promoted by hydrogen bonding in the backbone with nearby or distant amino acids Interactions that take place between side chains (not the backbone) =How separate peptide chains interact with each other Loop: a region with poorly defined structure, commonly found between regions of alpha-helices and beta-sheets 3 common ways to show protein structure Space-filled form Stick form Ribbon form Ribonuclease A Primary structure is held together by peptide bonds Figure 2.07: Peptide bond formation in the laboratory. MLSFALFGGLFVLIGTSRGSHSFTHTMSPRLHFRLYHGC...
View Full Document

This note was uploaded on 11/04/2011 for the course MMBIO 240 taught by Professor Bridgewater during the Fall '09 term at BYU.

Page1 / 40

Topic 4, protein folding.ppt.edu - Topic 4Protein Folding...

This preview shows document pages 1 - 10. Sign up to view the full document.

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