Flashcards
Biochemistry Lecture 2
Flashcards do conjunto (19)
- 1What is Primary Structure?Sequence of amino acids in a protein.
Determined by inherited genetic info.
1st AA: N-Terminus
Last AA: C-Terminus - 2What is Secondary structure?Coils and folds
Determined by hydrogen bonds between the polypeptide backbone. - 3What is Tertiary structure?Determined by interactions between side chains (R-groups)
- 4What is Quaternary structure?When two or more polypeptide chains form one macromolecule.
All the same interactions as Tertiary structure. - 5What is protein folding?Protein folding is the process by which a protein structure assumes its functional shape or conformation.
- 6What is the Protein Folding Problem?Understanding how a protein reaches its native structure from is AA sequence. We want to know how to translate DNA sequence into spatial information.
- 7What did Afinsen find from his experiment?The sequence of AA determines the 3D structure.
Protein Folding is a spontaneous process. - 8What is found from Levinthal's paradox?Protein folding cannot be a random search in conformational space. Therefore, proteins must fold in pre-arranged pathways.
- 9What are the four main protein folding models, based on the Anfinsen observations?Framework model.
Nucleation Growth.
Molten globules, hydrophobic collapse.
Jigsaw model. - 10What is the general view of Protein folding today?It is not a specific single pathway, but rather a large number of pathways funnelling down into the 'native state'.
This is called the folding free energy funnel. - 11What is a Chaperone?Proteins that help other proteins fold correctly
- 12What are the 2 major classes of Chaperones?Molecular chaperones.
Chaperonins. - 13What is the difference between a molecular chaperone and a chaperonin?Molecular chaperones act as monomers whereas chaperonins are large multi sub unit complexes.
- 14What is the function of chaperones?To help proteins in their folding process.
To unfold incorrectly folded proteins.
To protect proteins from interference during folding. - 15Give an example of protein folding diseases.Cystic Fibrosis
Marfan syndrome
Amyotonic lateral sclerosis
Alzheimer's
Parkinson's
Type II Diabetes
Cancer - 16What 3 methods are used in protein structure determination?X-ray crystallography
Nuclear Magnetic Resonance Spectroscopy
Cryo-electron microscopy - 17What is a domain?A segment of protein structure that is autonomously stable tertiary structure.
Stable by itself. - 18What is a motif/supersecondary structure?Recurring structural feature of protein composed of two or more secondary structure elements.
Not stable by itself. - 19How do proteins achieve their function?Through protein-ligand interactions.
Informações
- Descrição
- FlashCards sobre Biochemistry Lecture 2, criado por Katie-jae Dalton em 01-01-2020.
- Criado por
- Katie-jae Dalton
- Visualizações
- 3
- Avaliação
Mais sobre Protein folding and denaturation