Together, we related how biophysical and biochemical properties affected by
the SRY mutation relate to the regulation of a gene - regulatory network in a biological system.»
Not exact matches
Weiss has led a team of scientists through the discovery of multiple unique aspects of the
SRY protein
mutations, each with its own signature of defects in structure and function.
Mutations in
SRY alter the dynamics of male development during fetal life.
Mutations in the
SRY protein take place within an L - shaped protein architecture known as a high mobility group (HMG) box.
Mutations in
SRY have previously been found that impair the protein's ability to attach to DNA and activate specific genes involved in sex determination.
The new analysis is unusual in that the toddler's
SRY, containing a
mutation on the back surface of the protein, binds and bends DNA normally.
The toddler in the study had a
mutation in the gene encoding
SRY, or sex - determining region of the Y chromosome, a protein that initiates testes development in embryos.
Surprisingly, no one seems to have studied this family or their interesting
mutation from a biophysical perspective or toward the goal of how the
mutation might affect the gene - regulatory properties of
SRY.»