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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
- Where are we going in the study of biochemistry?
- Secondary structure: α-helix
- Proline special properties
- Amphipathic helices
- Secondary structure: ß-sheets
- Turns
- More on turns
- 'Special' secondary structure: collagen
- Collagen synthesis
- Stable protein folds
- Protein folds (1)
- Protein folds (2)
- Protein classification definitions
- Meaning of the protein classifications
- Lecture summary
Topics Covered
- Protein secondary structures: α helix, β-sheet, turns, and collagen
- Collagen properties
- The ‘protein fold’
- Protein arrangement according to type of fold, superfamily and family
Talk Citation
Feigenson, G.W. (2022, November 27). Observed protein structures [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 9, 2024, from https://doi.org/10.69645/GHWL3116.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
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0:00
Greetings. Welcome to this lecture series, Principles of Biochemistry.
I'm Jerry Feigenson, a professor in
the Department of Molecular Biology and Genetics at Cornell University in the US.
In the third lecture, you saw that researchers can learn a lot from knowing
the amino acid sequence without yet
knowing the full three-dimensional structure of a protein.
The basic principles of protein crystallography
to find the three-dimensional structure were described,
six categories of interactions that determine protein structure were shown,
and you saw the consequences of the real size of atoms and peptide bond constraints,
which together greatly restrict the possible structures of proteins.
0:53
In this fourth lecture,
you will learn about protein secondary structures, alpha-helices, beta-sheets, turns,
and collagen, and you will learn that what we call the protein fold is stable,
and only about 1,400 different protein folds exist.
Proteins can be arranged according to the type of fold,
the superfamily and the family.
1:19
Before we get to protein folds,
let me show you where we are in the study of biochemistry.
We are here, protein structure.
We will soon be looking at enzyme catalysis,
then regulation of enzymes,
then carbohydrates and lipids and membranes, and metabolism.
In fact, for metabolism,
we will spend quite a number of lectures.
The interconnections and control of metabolism are based on proteins.
So we're here now with protein structure, and then soon,
we will notice what structures we observe,
we'll study how catalysts work,
and how enzymes are controlled.