Answer:
// program in C++.
#include <bits/stdc++.h>
using namespace std;
int main() {
// variable
int num;
cout<<"Enter the number between 20 and 98: ";
// read number
cin >> num;
while(num<20||num>98)
{
cout<<"Wrong input!!enter number between 20-98 only:";
cin>>num;
}
cout<<"The output is: ";
while(num % 10 != num /10)
{
// print numbers.
cout<<num<<" ";
// update num.
num--;
}
// display the number.
cout<<num<<endl;;
return 0;
}
Explanation:
Read a number from user and assign it to variable "num".Check if entered number is in between 20-98 or not.If input number is less than 20 or greater than 98 then ask again to enter a number between 20-98 until user enter a valid input.Then print the countdown from input number till both the digit of number are same.
Output:
Enter the number between 20 and 98: 99
Wrong input!!enter number between 20-98 only:12
Wrong input!!enter number between 20-98 only:93
The output is: 93 92 91 90 89 88
Enter the number between 20 and 98: 77
The output is: 77
Answer:
yes it can it shows u what you did wrong or what you did right
Explanation:
brainlet me please
Answer:The allosteric inhibitors of integrase (termed ALLINIs) interfere with HIV replication by binding to the viral-encoded integrase (IN) protein. Surprisingly, ALLINIs interfere not with DNA integration but with viral particle assembly late during HIV replication. To investigate the ALLINI inhibitory mechanism, we crystallized full-length HIV-1 IN bound to the ALLINI GSK1264 and determined the structure of the complex at 4.4 Å resolution. The structure shows GSK1264 buried between the IN C-terminal domain (CTD) and the catalytic core domain. In the crystal lattice, the interacting domains are contributed by two different dimers so that IN forms an open polymer mediated by inhibitor-bridged contacts; the N-terminal domains do not participate and are structurally disordered. Engineered amino acid substitutions at the inhibitor interface blocked ALLINI-induced multimerization. HIV escape mutants with reduced sensitivity to ALLINIs commonly altered amino acids at or near the inhibitor-bound interface, and these substitutions also diminished IN multimerization.
Explanation:
