Protein Strctr Word Scramble
|
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.
Normal Size Small Size show me how
Normal Size Small Size show me how
Question | Answer |
4 Molecular Organization Levels of Proteins | Primary Secondary Tertiary Quaternary |
Functions of Proteins | Signaling, Transport, Catalysis, Movement, Structure, Regulation |
Primary Structure | Sequence of Amino Acids. Known primary structure may be used to diagnose or study disease. |
Amino Acids are joined by _________ bonds. | Peptide |
How are peptide bonds formed? | N terminus to C terminus |
Limitations of DNA sequencing | -Can't predict the disulfide bonds -Can't identify post-translational modifications |
AA sequence is determined by: | sequencing the coding region of DNA |
Secondary Structures | alpha-helix, beta-sheets, beta-bends |
alpha-helix | -spiral, tightly packed structure -side chains extend outward |
protein contents of alpha helices | -keratins are nearly entirely alpha-hilical -myoglobin contains only 8% alpha-helices |
alpha helix hydrogen bonding | occurs between the carbonyl oxygen and the amide hydrogen of the backbone |
disrupts alpha helix formation | -proline -large number of charged AA that form ionic bonds -large numbers of AA with bulky side chains |
beta sheets | -appear pleated -hydrogen bonds are perpendicular to polypeptide backbone -parallel or anti-parallel |
interchain bonds (beta sheets) | separate polypeptide chains |
intrachain bonde (beta sheets) | single polypeptide |
beta bends | -reverse turns -generally composed of 4 amino acids (often includes proline or glycine) |
tertiary structure | -folding of domains and final arrangement of domains -Primary structure of polypeptide chain determines tertiary structure |
Domains | fundamental functional 3D structural units of polypeptide |
core domain (tertiary) | is built from a combination of motifs |
The Four types of interactions that cooperate to stabilize tertiary structure of proteins | -Disulfide bonds -Hydrophobic interactions -Hydrogen bonds -Ionic interactions |
Disulfide bond | formed by sulfhydryl groups (-SH) of two Cys residues |
Hydrophobic interactions | -form between nonpolar side chains |
process of folding | -process of folding in vivo often begins co-translationally from N-terminus |
chaperones | -“heat shock proteins” - involved in various stages of folding -Keep protein unfolded -Increase the rate -Protect from unproductive interactions |
examples of chaperones | GroEL, GroES |
Denaturation | -unfolding and disorganizing of protein’s secondary and tertiary structures -done by heat, chemicals, and ions of heavy metals -can be reversible or irreversible |
Quality control | misfolded proteins are tagged and degraded in the cell |
Amyloids | -Accumulation of spontaneously aggregating proteins caused by misfolding -Associated with degenerative diseases like Alzheimer's disease. |
Components of amyloid plaque in Alzheimer's | -amyloid precursor protein -neurofibrillary tangles in the brain caused by abnormal form of tau protein |
Prion protein (PrP) | -Infectious protein produced in brain, resistant to proteolysis -causes transmissible spongiform encephalopathies (TSEs) -Creutzfeldt-Jakob disease in humans -Scrapie in sheep -Bovine spongiform encephalopathy “mad cow disease” in cattle |
Created by:
1526302205
Popular Chemistry sets