Question

Can someone help me....? Thanks

Tracking Changes Compare Protect Comments u C #つ bits tht Hy mak

Answer 1

Actually the question is not in a clear way..what I understand from this was answered below.

What holds the helix together?

The local region of the polypeptide chain will fold into either an alpha helix or a beta sheet. These structures make the secondary structures. The secondary structures of some proteins is essentially all alpha helices. These secondary structures are held together by Hydrogen bonds.

What holds the tertiary structure together?

Disulfide bridges with the Hydrogen bonds can bring together two parts of a chain that are some distance away in terms of sequence.salt bridges ionic interactions between positively and negatively charged does on amino acid side chains also help to stabilize the tertiary structure of a protein.

What holds the quarternary structures of a protein together?

These chains are held together to form the larger protein by bonds that exist between the side groups of different chains. As in the tertiary structure the bond involved in holding these separate chains together can be van der waals force,,hydrogen bonds, ionic bonds or sometime covalent bonds.

PROTEIN DOMAIN

A protein domain is a conserved part of a given protein sequence and tertiary structure that can evolveand exist independently of the rest of the protein chain.each protein form a compact 3dimensional structure and often can be independently stable and folded. Many proteins consist of several domains. One domain may appear in a variety of different proteins.

NATIVE PROTEIN

Native protein are the proteins which are on their folded or assembled form and they are fully functional. They will not affected by denaturing agents such as chemical,heat,enzymes,or anything. These proteins will have intact structure.

When can a protein be denatured?

Denaturation of protein include disruption and destruction of both the secondary and tertiary structure. Denaturation reactions are not strong enough typo break the poly peptide bond, the sequence of amino acid remains the same after the denaturation process. Denaturation disrupts the normal alpha helixand beta sheets in a protein and uncoil it into a random shape. Denaturation occurs because the bonding interactions responsible for the secondary structure are disrupted. In tertiary structure there are 4 types of bonding interaction between side chains including Hydrogen bonding, salt bridges, disulfide bonds and non polar hydrophobic interactions which may disrupted. Therefore a variety of reagents and condition can cause denaturation. The most common observation in the denaturation process is the coagulation of the protein.

How do proteins know how to reassemble?

Protein carry out immense range of actions within living Organism. In stomach there are different types of enzymes such as rennin, trypsin, pepsin etc. The protein are Brkon down Into the constituent amino acid in our digestive system. They are not reassembled into the same position that one had taken. They are bio synthesised into the protein specific to our individual tissues and feels. This is due to the Specific mRNA s transcribed in our different tissues.which have the condoms specific for the protein required in our system.  

If you want further answers or description make the questions in a clearer way and repost.