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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
- Prior to 3D, find the primary protein structure
- Isoenzyme example: hexokinase
- Information from the primary protein structure (1)
- Information from the primary protein structure (2)
- Information from the primary protein structure (3)
- Bioinformatics
- Atomic level' protein 3D structure
- The diffraction experiment (1)
- The diffraction experiment (2)
- X-ray diffraction results of myoglobin
- 6 catergories of interactions (1)
- 6 catergories of interactions (2)
- Peptide bond constraints
- Deviations from ground state
- Peptide bond constraints & finite size of atoms
- The Ramachandran map: steric hindrance
- The Ramachandran map: let's add more reality
- Lecture summary
Topics Covered
- Primary protein structure
- X-ray diffraction and protein 3D structure
- Interactions within proteins
- Peptide bond constraints
- Ramachandran maps
Talk Citation
Feigenson, G.W. (2022, November 27). Protein structure principles [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 22, 2024, from https://doi.org/10.69645/UPJH8100.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.
My name is Jerry Feigenson.
I am a professor in
the Department of Molecular Biology and Genetics at Cornell University in the USA.
In the second lecture,
you saw some properties of each of the 20 amino acid residues that are found in proteins.
You saw the peptide bond formation that creates the protein polymer
and you saw the hydrophobic effect that drives water soluble proteins to fold,
and you saw that once we start to examine a real protein,
myoglobin, we see the need to know the three-dimensional structure.
0:44
In this third lecture,
you will learn before finding the protein three-dimensional structure,
just knowing the amino acid sequence is useful,
and you will see how x-ray diffraction is used to find protein 3D structure.
I will show you the six categories of
interactions that determine protein structure and action
and you will see the structural consequences of
the peptide bond and the real size of atoms.
1:12
Prior to finding the three-dimensional structure,
we can find the primary protein structure,
which means the amino acid sequence.
It used to be that researchers used protein-based methods.
They would start with protein,
put it into an automated protein sequenator,
and find the sequence of amino acids in the actual protein.
This was a very useful research method,
but it's actually very difficult to do this.
Let's label this method difficult.
It might surprise you that
most amino acid sequences are determined nowadays in a different way.
In fact, what's done nowadays is to find the sequence of amino acids.
We first find the part of DNA that
codes for this protein and then sequence the nucleotides.
The nucleotides are far easier to
measure their sequence than it is for amino acids in a protein.
So we sequence the nucleotides and we call this method easy.
So that's how we find the amino acid sequence. So let's do that.
Well, we run into an interesting behavior and here's a bit of jargon.
We use the term isozyme or equivalent isoenzyme or isoform.
It means from the same organism,
analytically and structurally similar enzymes,
but the amino acid sequence is slightly different.
Let me give you an example.
Suppose we determine the amino acid sequence for myoglobin from many different tissues.
Well, no matter what's the source of myoglobin,
we find the same amino acid sequence.
If we do this for some other proteins,
we find a different result.
For example, the enzyme hexokinase from different tissues,
we find different amino acid sequences.
That means, different isoforms or isozymes.