Beruflich Dokumente
Kultur Dokumente
DI SUSUN OLEH :
DOSEN PENGAMPU :
UNIVERSITAS JAMBI
2019
PROBLEM
22.18. P.W. Seakins, M.J. Pilling, L.T. Niiranen, D. Gutman, and L.N. Krasnoperov (J.
Phys. Chem. 96, 9847 (1992)) measured the forward and reverse rate constants for the
gas-phase reaction C2H5(g) + HBr(g) → C2H6(g) + Br(g) and used their findings to
compute thermodynamic parameters for C2H5. The reaction is bimolecular in both
directions with Arrhenius parameters A = 1.0 × 109 dm3 mol−1 s −1 , Ea = −4.2 kJ
mol−1 for the forward reaction and k′ = 1.4 × 1011 dm3 mol−1 s −1 , Ea = 53.3 kJ
mol−1 for the reverse reaction. Compute ∆f H 7 , S 7 m, and ∆fG7 of C2H5 at 298 K.
ANSWER:
22.34. Propose a set of experiments in which analysis of the line-shapes of NMR
transitions (Section 15.7) can be used to monitor fast events in protein folding and
unfolding. What are the disadvantages and disadvantages of this NMR method over
methods that use electronic and vibrational spectroscopy?
ANSWER: analysis of NMR line shapes can be used to infer time scales of protein folding
or unfolding steps. protons ( or other nuclei,for that matter ) that have different chemical
shifts in folded and unfolded proteins will yield a single peak if the time scale for
interconversion. ( i.e.for folding or ufolding ) is comparable to or less than the reciprocal of
the two peaks frequency difference. Monitoring the change from two peaks (indicating that a
sample contains both folded and unfolded proteins, which migh be observed at one
temperature) to abroad single peak (indicating fast interconversion, which might be the case
at a higher temperature) can allow the determination oftime constan for the conversion.one
advantage of NMR over vibrational or electronic spectroscopy is that the radiation used to
probe the system is much less energetic, and therefore much less likely to alter the folding or
unfolding process it is designed to investigate.the line shapes strategy cannot be used to
investigate processes as fast as those accessible by elektonic or vibrational spectroscopy
analisis bentuk garis NMR dapat digunakan untuk menyimpulkan skala waktu langkah-
langkah pelipatan protein atau lipatan. proton (atau nukleus lainnya, dalam hal ini) yang
memiliki perubahan kimiawi yang berbeda pada protein yang terlipat dan tidak dilipat akan
menghasilkan puncak tunggal jika skala waktu untuk interkonversi. (mis. untuk melipat atau
membuat cetakan) sebanding dengan atau kurang dari kebalikan dari dua perbedaan frekuensi
puncak. Memantau perubahan dari dua puncak (menunjukkan bahwa sampel mengandung
protein yang terlipat dan tidak dilipat, yang dapat diamati pada satu suhu) ke puncak tunggal
di luar negeri (menunjukkan interkonversi cepat, yang mungkin terjadi pada suhu yang lebih
tinggi) dapat memungkinkan penentuan waktu. Konstan untuk konversi. Satu keuntungan
dari NMR daripada spektroskopi vibrasi atau elektronik adalah bahwa radiasi yang digunakan
untuk menyelidiki sistem jauh lebih sedikit energik, dan oleh karena itu jauh lebih kecil
kemungkinannya untuk mengubah proses pelipatan atau penguraian yang dirancang untuk
menyelidiki. tidak dapat digunakan untuk menyelidiki proses secepat yang dapat diakses oleh
spektroskopi elektonik atau getaran.
23.18 Conventional equilibrium considerations do not apply when a reaction is being driven by
light absorption. Thus the steady-state concentration of products and reactants might differ
significantly from equilibrium values. For instance, suppose the reaction A → B is driven by light
absorption and that its rate is Ia, but that the reverse reaction B → A is bimolecular and second-
order with a rate k[B]2 . What is the stationary state concentration of B? Why does this
‘photostationary state’ differ from the equilibrium state?
ANSWER :