The amide bond in a protein has a negative δg°' of hydrolysis under physiological conditions in the cell. in other words, the peptide bond is thermodynamically unstable, yet proteins are an important component of the cell and do not just fall apart sponstaneously. why?

The hydrolysis rate is significantly low because the energy of the transition state for hydrolysis is significantly high

Explanation:

In the given problem,  It was stated that the peptide bond is not stable thermodynamically. Peptide bonds are typically formed between molecules with carboxyl groups and molecules with amino groups. Therefore, it can be inferred that the hydrolysis rate is significantly low because the energy of the transition state for hydrolysis is significantly high.

ch3 [ch2]14cooh

explanation:

when 25.0 ml of 0.700 mol/l naoh was mixed in a calorimeter with 25.0 ml of 0.700 mol/l hcl, both initially at 20.0 °c, the temperature increased to 22.1 °c. the heat capacity of the calorimeter is 279 j/°c.

the equation for the reaction is:

naoh + hcl → nacl + h₂o

moles of hcl = 0.0250 l hcl ×

0.700

mol hcl

1 l hcl = 0.0175 mol hcl

volume of solution = (25.0 + 25.0) ml = 50.0 ml

mass of solution = 50.0 ml soln ×

1.00

ml soln

= 50.0 g soln

δt=t2-t1

= (22.1 – 20.0) °c = 2.1 °c

the heats involved are

heat from neutralization + heat to warm solution + heat to warm calorimeter = 0

q1+q2+q3=0

nδh+mcδt+cδt=0

0.0175 mol ×

δh

+ 50.0 g × 4.184 j·g⁻¹°c⁻¹ × 2.1 °c + 279 j°c⁻¹ × 2.1 °c = 0

0.0175 mol ×

δh

+ 439.32 j + 585.9 j = 0

0.0175 mol ×

δh

= -1025.22 j

δh=1025.22j0.0175 mol= -58 600 j/mol = -58.6 kj/mol