protein function with DTT treatment

Discussion of all aspects of biological molecules, biochemical processes and laboratory procedures in the field.

Moderators: honeev, Leonid, amiradm, BioTeam

Post Reply
Posts: 5
Joined: Tue Oct 07, 2008 10:18 am

protein function with DTT treatment

Post by proteinz » Mon Oct 13, 2008 3:48 pm

hi all, no idea where to post this> but has any one ever heard of a protein that increases its chaperone activity following reduction with 5mM DTT?

Posts: 1
Joined: Tue Oct 14, 2008 10:54 am

Re: protein function with DTT treatment

Post by joycelorenza » Tue Oct 14, 2008 11:10 am

Proteins are large organic compounds made of amino acids arranged in a linear chain and joined together by peptide bonds between the carboxyl and amino groups of adjacent amino acid residues. The sequence of amino acids in a protein is defined by a gene and encoded in the genetic code. Although this genetic code specifies 20 "standard" amino acids plus selenocysteine and - in certain archaea - pyrrolysine, the residues in a protein are sometimes chemically altered in post-translational modification.
joyce lorenza
social advertisers

Post Reply

Who is online

Users browsing this forum: No registered users and 19 guests