comparable to the very high concentrations (∼3–30 μM) of themajor tRNA terjemahan - comparable to the very high concentrations (∼3–30 μM) of themajor tRNA Bahasa Indonesia Bagaimana mengatakan

comparable to the very high concent

comparable to the very high concentrations (∼3–30 μM) of the
major tRNA species found in rapidly growing E. coli (31).
This concentration scale can be converted to a proteome
fraction (φM) of tRNA-affiliated proteins (referred to henceforth
as T-proteins). This class of proteins includes EF-Tu and the
tRNA synthetases, which are found at constant ratio to EF-Tu in
E. coli (15). Considering the protein mass of EF-Tu and tRNA
synthetases, we obtain a scale of φM ≈ 0.02. This is consistent
with the measured proteome fraction of T-proteins in the cell,
which ranges between 5% and 13% depending on growth conditions
and corresponds to ∼60% of the ribosomal protein mass
(Fig. 1A). As the estimated Michaelis constant corresponds to
the concentration at which translation would proceed at half of
its maximal speed, these numbers indicate that the translation
speed ranges between 70% and 86% of its maximum, consistent
with earlier estimates for Salmonella (16). Our estimate of the
Michaelis constant thus suggests that translation indeed operates
close to the diffusion limit and that macromolecular crowding
imposes a substantial cost to the cell by setting a large scale for
the required allocation of T-proteins.
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Hasil (Bahasa Indonesia) 1: [Salinan]
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comparable to the very high concentrations (∼3–30 μM) of themajor tRNA species found in rapidly growing E. coli (31).This concentration scale can be converted to a proteomefraction (φM) of tRNA-affiliated proteins (referred to henceforthas T-proteins). This class of proteins includes EF-Tu and thetRNA synthetases, which are found at constant ratio to EF-Tu inE. coli (15). Considering the protein mass of EF-Tu and tRNAsynthetases, we obtain a scale of φM ≈ 0.02. This is consistentwith the measured proteome fraction of T-proteins in the cell,which ranges between 5% and 13% depending on growth conditionsand corresponds to ∼60% of the ribosomal protein mass(Fig. 1A). As the estimated Michaelis constant corresponds tothe concentration at which translation would proceed at half ofits maximal speed, these numbers indicate that the translationspeed ranges between 70% and 86% of its maximum, consistentwith earlier estimates for Salmonella (16). Our estimate of theMichaelis constant thus suggests that translation indeed operatesclose to the diffusion limit and that macromolecular crowdingimposes a substantial cost to the cell by setting a large scale forthe required allocation of T-proteins.
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Hasil (Bahasa Indonesia) 2:[Salinan]
Disalin!
sebanding dengan konsentrasi yang sangat tinggi (~3-30 M) dari
spesies tRNA utama yang ditemukan dalam berkembang pesat E. coli (31).
skala Konsentrasi ini dapat dikonversi ke proteoma
fraksi (φM) protein tRNA berafiliasi (disebut selanjutnya
sebagai T-protein). Kelas ini meliputi protein EF-Tu dan
sintetase tRNA, yang ditemukan pada rasio konstan untuk EF-Tu di
E. coli (15). Mengingat massa protein EF-Tu dan tRNA
sintetase, kita memperoleh skala φM ≈ 0.02. Ini konsisten
dengan fraksi proteome diukur dari T-protein dalam sel,
yang berkisar antara 5% dan 13% tergantung pada kondisi pertumbuhan
dan sesuai dengan ~60% dari massa protein ribosom
(Gbr. 1A). Sebagai estimasi berkoresponden konstan Michaelis ke
konsentrasi di mana terjemahan akan berlangsung pada setengah dari
kecepatan maksimal yang, angka-angka ini menunjukkan bahwa terjemahan
kecepatan berkisar antara 70% dan 86% dari maksimum, konsisten
dengan perkiraan sebelumnya untuk Salmonella (16). Perkiraan kami dari
Michaelis konstan sehingga menunjukkan bahwa terjemahan memang beroperasi
mendekati batas difusi dan crowding makromolekul
membebankan biaya besar ke sel dengan menetapkan skala besar untuk
alokasi yang diperlukan dari T-protein.
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