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1. Introduction to biochemistry
- Prof. Gerald W. Feigenson
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2. Amino acids and peptides
- Prof. Gerald W. Feigenson
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3. Protein structure principles
- Prof. Gerald W. Feigenson
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4. Observed protein structures
- Prof. Gerald W. Feigenson
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5. Protein folds and IV structure
- Prof. Gerald W. Feigenson
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6. Protein stability and folding
- Prof. Gerald W. Feigenson
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7. Haemoglobin structure and stability
- Prof. Gerald W. Feigenson
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8. Enzyme specificity and catalysis
- Prof. Gerald W. Feigenson
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9. Enzyme kinetics (Michaelis-Menten)
- Prof. Gerald W. Feigenson
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10. Enzyme inhibition; chymotrypsin
- Prof. Gerald W. Feigenson
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11. Enzyme regulation and coenzymes
- Prof. Gerald W. Feigenson
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12. Lipids, biomembranes and membrane proteins
- Prof. Gerald W. Feigenson
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13. Structure and function of carbohydrates
- Prof. Gerald W. Feigenson
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14. Metabolism principles
- Prof. Gerald W. Feigenson
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15. Glycolysis - energy and useful cell chemicals
- Prof. Gerald W. Feigenson
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16. Glycolysis control
- Prof. Gerald W. Feigenson
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17. Metabolism of pyruvate and fat
- Prof. Gerald W. Feigenson
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18. Urea cycle; oxidative phosphorylation 1
- Prof. Gerald W. Feigenson
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19. Urea cycle; oxidative phosphorylation 2
- Prof. Gerald W. Feigenson
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20. Light-driven reactions in photosynthesis
- Prof. Gerald W. Feigenson
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21. Gluconeogenesis and the Calvin cycle
- Prof. Gerald W. Feigenson
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22. Synthesis of lipids and N-containing molecules 1
- Prof. Gerald W. Feigenson
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23. Synthesis of lipids and N-containing molecules 2
- Prof. Gerald W. Feigenson
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24. Hormone mechanisms
- Prof. Gerald W. Feigenson
Printable Handouts
Navigable Slide Index
- Introduction
- Lecture outline
- Consider the protein folding/unfolding process
- Thermodynamics view reveals driving force (1)
- Thermodynamics view reveals driving force (2)
- Fold or unfolded, essentially all H-bonds are made
- How to describe protein stability with a graph
- Denaturation and renaturation
- Jargon digression
- A key experiment in the history of biochemistry
- Why is it amazing that Mb can fold?
- Real world: refolding not so simple
- Real world: two enzymes speed up folding
- Real world: molecular chaperones
- How do molecular chaperones work?
- Beyond structure: motions within proteins
- What is the 'pathway' of protein folding?
- Protein 3D structure from AA sequence?
- Protein classification by function
- Protein classification by complexity
- Lecture summary
Topics Covered
- Protein stability
- Folding and refolding
- Molecular chaperones
- Motions within proteins
- Protein classification by function
- Protein classification by complexity
Talk Citation
Feigenson, G.W. (2022, November 27). Protein stability and folding [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 6, 2024, from https://doi.org/10.69645/FSUU3391.Export Citation (RIS)
Publication History
Financial Disclosures
- Gerald Feigenson has no commercial/financial relationships to disclose.
Request access to the Principles of Biochemistry lecture series, an extensive introductory to the field of biochemistry. An HSTalks representative will contact you with more information about this series and getting unrestricted access to it.
A selection of talks on Biochemistry
Transcript
Please wait while the transcript is being prepared...
0:00
Greetings. Welcome to this principles of biochemistry lecture series.
I am Jerry Feigenson.
I am a professor in the Department of
Molecular Biology and Genetics at Cornell University in the USA.
In the fifth lecture,
you saw that multiple folds can occur in a single polypeptide chain
and that more than one chain can associate in what is called quaternary structure.
That quaternary structure, can be very stable or else transient,
forming in order to transmit a signal.
0:37
In this lesson, you will learn that protein structure is stable,
but not very stable and you will learn that all information needed to fold
a protein into its stable structure is in the amino acid sequence.
Proteins fold up in roughly seconds to minutes,
but we calculate that to be much faster than they should be taking.
In order to fold into their stable structure,
many proteins require some help.
We will see that proteins have internal motions and that
proteins can be classified according to function and complexity.
1:19
Let's consider the protein folding and unfolding process.
On the left is a protein in water not folded and on the right,
you see some structure and this picture on the right,
reflects the folded protein.
In water, the unfolded protein has many different structures,
rapidly interchanging and on the right,
the folded protein, it's a structure that's relatively fixed.