Courtemanche, Naomi, Barrick, Doug
Although the folding of α-helical repeat proteins has been well characterized, much less is known about the folding of repeat proteins containing β-sheets. Here we investigate the folding...
Street, Timothy O., Bradley, Christina Marchetti, Barrick, Doug
Changes in protein stability can be achieved by making substitutions that increase or decrease the available conformations of the unfolded protein without altering the conformational freedom of the...
Structure and stability of the ankyrin domain of the Drosophila Notch receptor (2003)
Zweifel, Mark E., Leahy, Daniel J., Hughson, Frederick M., Barrick, Doug
The Notch receptor contains a conserved ankyrin repeat domain that is required for Notch-mediated signal transduction. The ankyrin domain of Drosophila Notch contains six ankyrin sequence repeats...
Quantitative analysis of ribosome binding sites in E.coli (1994)
Barrick, Doug, Villanueba, Keith, Childs, John, Kalil, Rhonda, Schneider, Thomas D., Lawrence, Charles E., ...
185 clones with randomized ribosome binding sites, from position −11 to 0 preceding the coding region of β-galactosidase, were selected and sequenced. The translatlonal yield of each clone was...
Structure and stability of a partly folded intermediate of sperm whale apomyoglobin / (1993)
Submitted to the Department of Biochemistry.
Bertagna, Angela M., Barrick, Doug
Acid-induced unfolding of apomyoglobin (apoMb) proceeds in a multistate process involving at least one equilibrium intermediate (I) at pH 4.2. The structure of the I form has been investigated...
An experimentally determined protein folding energy landscape
Mello, Cecilia C., Barrick, Doug
Energy landscapes have been used to conceptually describe and model protein folding but have been difficult to measure experimentally, in large part because of the myriad of partly folded protein...
Bertagna, Angela M., Barrick, Doug
Acid-induced unfolding of apomyoglobin (apoMb) proceeds in a multistate process involving at least one equilibrium intermediate (I) at pH 4.2. The structure of the I form has been investigated...
An experimentally determined protein folding energy landscape
Mello, Cecilia C., Barrick, Doug
Energy landscapes have been used to conceptually describe and model protein folding but have been difficult to measure experimentally, in large part because of the myriad of partly folded protein...
Predicting coupling limits from an experimentally determined energy landscape
Street, Timothy O., Bradley, Christina M., Barrick, Doug
Repeat proteins are composed of tandem structural modules in which close contacts do not extend beyond adjacent repeats. Despite the local nature of these close contacts, repeat proteins often unfold...
Street, Timothy O., Bradley, Christina Marchetti, Barrick, Doug
Changes in protein stability can be achieved by making substitutions that increase or decrease the available conformations of the unfolded protein without altering the conformational freedom of the...
Structure and stability of a partly folded intermediate of sperm whale apomyoglobin /
Submitted to the Department of Biochemistry and The Committee on Graduate Studies of Stanford University.
Measuring the stability of partly folded proteins using TMAO
Mello, Cecilia C., Barrick, Doug
Standard methods for measuring free energy of protein unfolding by chemical denaturation require complete folding at low concentrations of denaturant so that a native baseline can be observed....
Structure and stability of the ankyrin domain of the Drosophila Notch receptor
Zweifel, Mark E., Leahy, Daniel J., Hughson, Frederick M., Barrick, Doug
The Notch receptor contains a conserved ankyrin repeat domain that is required for Notch-mediated signal transduction. The ankyrin domain of Drosophila Notch contains six ankyrin sequence repeats...
Courtemanche, Naomi, Barrick, Doug
Although the folding of α-helical repeat proteins has been well characterized, much less is known about the folding of repeat proteins containing β-sheets. Here we investigate the folding...