Key numbers in Biochemistry

Key numbers in Biochemistry für die Vorlesung Grundlagen der Biologie II: Molekularbiologie und Biochemie, Dozent Rudi Glockshuber

Key numbers in Biochemistry für die Vorlesung Grundlagen der Biologie II: Molekularbiologie und Biochemie, Dozent Rudi Glockshuber


S. W.
This flashcard set provides essential numerical data for biochemistry at the university level, focusing on key metrics like enzyme kinetics, DNA structure, and cellular dimensions. It covers crucial values such as acceleration factors, diffusion limits, and protein concentrations, offering insights into molecular biology and cellular processes. Ideal for students and researchers, this flashcard set helps understand the quantitative aspects of biochemical reactions and cellular components, making complex data more accessible and easier to grasp.
Karten
38
Lernende
2
Sprache
Englisch
Kategorie
Biologie
Stufe
Universität
Erstellt / Aktualisiert
24.10.2018 / 24.01.2021

Lernkarten

Avogadro number

\(N_A = 6.0\cdot 10^{23}\ mol^{-1}\)

Proton concentration

\(\mathrm{[H^+]=10^{-pH}\ M\\pH=-\log[H^+]}\)

What does a two-state equilibrium (\(A\leftrightarrow B\)) at 25 °C with an equilibrium constant Keq of \(\frac{[A]}{[B]}=\frac{10}{1}\) indicate?

It indicates that A is 5.7 kJ/mol more stable than B; every order of magnitude of Keq translates into 5.7 kJ/mol \(\mathrm{(\Delta G=-RT\ln K_{eq}) \rightarrow if\ K_{eq}=1000:1, \Delta G =3\cdot 5.7\ kJ/mol=17.1\ kJ/mol}\)

The same applies to enzymes: if the activation energy of a reaction is lowered by 5.7 kJ/mol by an enzyme, the reaction becomes 10 times faster.

Time for an average protein to traverse an E. coli cell by free diffusion

\(\sim 10\ \mathrm{ms}\)

Time for an average protein to traverse a HELA cell (Menschliche Epithel Zelle) by free diffusion

\(\sim10\) s

Size  and volume of an E. coli cell

~3 x 0.5 \(\mu\)m / 1 \({\mu m}^3\)

size and volume of a yeast cell (S. cerevisiae)

5 - 10 \(\mu m\ 40\ {\mu m}^3\)

Size and volume of mitochondria

\(1\ \mu m;\ 1{\mu m}^3\)

Size of animal cells

\(10-100\ \mu m\)

Diameter of the cell nucleus

\(2-10\ \mu m\)

Genome size / number of protein-encoding genes: Mycoplasma mycodes

0.57 Mb / 473 (smallest known genome)

Genome size / number of protein-encoding genes: E. coli

4.6 Mb / 4300

Genome size / number of protein-encoding genes: S. cerevisiae (yeast)

12.5 Mb / 6000

Genome size / number of protein-encoding genes: H. sapiens

3000 Mb / ~20'000 - 25'000

Length of a C-C bond

1.54 A = 0.154 nm

Distance between the heavy atoms (donor and acceptor) of a hydrogen bond in proteins and nucleic acids

2.8 A

Length of the \(\alpha\)-helix

1.5 A per amino acid

Amino acids per \(\alpha\)-helix turn

3.4

Length of a \(\beta\)-strand (extended polypeptide chain)

3.3 - 3.5 A per amino acid

Average mass of an amino acid in a protein

110 Da

Average length of cellular proteins

~300 - 350 amino acids (~35 kDa)

Diameter of a folded protein with 100 amino acids

~30 A

Distance between superposed base pairs in the DNA double helix (B-DNA)

3.3 A

Diameter of the DNA double helix (B-DNA)

20 A

Number of base pairs per turn of the double helix (B-DNA)

10.5

Average mass of a DNA base pair

~650 Da

Total hypothetical extended length of human genomic DNA

~1 m

Total intracellular protein concentration

~200 - 300 mg/mL, 2 - 4 million proteins per \({\mu m}^3\)

Rule of thumb: a protein concentration of 1\(\mu M\) corresponds to 1'000 molecules per E. coli cell (volume \(\sim 10\ {\mu m}^3\))

Total and individual metabolite concentration

Der Metabolit (griechisch μεταβολίτης metabolítes, deutsch ‚der Umgewandelte‘, Plural: Metaboliten) ist ein Zwischenprodukt (Intermediat) in einem meist biochemischenStoffwechselweg.

total: ~300 mM

individual metabolites: \(0.1\ \mu M\ -\ 100\ mM\)

In E. coli, individual metabolite concentrations are generally higher than their KM values.

Equilibrium thermodynamics, energetics of ATP hydrolysis \((\Delta G^{0'})\)

\(\Delta G^{0'}=-30.5\ kJ/mol\)

Dissociation constants of natural protein-ligand interactions

\(10^{-3}-10^{-15}\ M\)

On-rates of physiological protein-ligand interactions

\(10^3-10^9\ M^{-1}s^{-1}\)

Half-lives of spontaneous dissociation of protein-ligand complexes

\(\sim 10\ ms\rightarrow 10^6\) years

Upper (diffusion) limit of second-order rate constants in water (small molecules)

\(\sim 10^10\ M^{-1}s^{-1}\)

KM values of natural enzyme/substrate pairs

\(0.1\ \mu M-100\ mM\)

kcat values of natural enzymes

\(0.01-10^6\ s^{-1}\)

Upper (diffusion) limit of catalytic efficiency (kcat/KM)

\(\sim 10^9\ M^{-1}s^{-1}\)

Acceleration factors (kcat / kuncat) of natural enzymes

\(10^3-10^17\)

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