D. Barrick

发表

Urea unfolding of peptide helices as a model for interpreting protein unfolding.

R. L. Baldwin, J. M. Scholtz, D. Barrick, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Extreme stability in de novo-designed repeat arrays is determined by unusually stable short-range interactions

David Baker, Doug Barrick, Fabio Parmeggiani, 2018, Proceedings of the National Academy of Sciences.

The association rate constant for heme binding to globin is independent of protein structure.

D. Barrick, J. Olson, M. Hargrove, 1996, Biochemistry.

Protein folding and stability using denaturants.

D. Barrick, Timothy O. Street, N. Courtemanche, 2008, Methods in cell biology.

Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability

Doug Barrick, D. Barrick, T. Dao, 2015, Proceedings of the National Academy of Sciences.

The consequences of cavity creation on the folding landscape of a repeat protein depend upon context

Zackary White, Sol M. Gruner, Catherine A. Royer, 2018, Proceedings of the National Academy of Sciences.

Consensus sequence design as a general strategy to create hyperstable, biologically active proteins

D. Barrick, M. Sternke, K. Tripp, 2019, Proceedings of the National Academy of Sciences.

Consensus sequence design as a general strategy to create hyperstable, biologically active proteins

Doug Barrick, D. Barrick, M. Sternke, 2018, Proceedings of the National Academy of Sciences.

Vibrational circular dichroism measurements of ligand vibrations in haem and non-haem metalloenzymes.

D. Barrick, S. Asher, R. Bormett, 1994, Faraday discussions.

Dissecting and Circumventing the Requirement for RAM in CSL-Dependent Notch Signaling

D. Barrick, Scott E. Johnson, 2012, PloS one.

Thermodynamic analysis of the CSL x Notch interaction: distribution of binding energy of the Notch RAM region to the CSL beta-trefoil domain and the mode of competition with the viral transactivator EBNA2.

D. Barrick, Raphael Kopan, M. Ilagan, 2010, The Journal of biological chemistry.

Quantitative dissection of the Notch:CSL interaction: insights into the Notch-mediated transcriptional switch.

D. Barrick, Raphael Kopan, O. Lubman, 2007, Journal of molecular biology.

Depletion and replacement of protein metal ligands.

D. Barrick, D Barrick, 1995, Current opinion in biotechnology.

Mapping the Deltex-binding surface on the notch ankyrin domain using analytical ultracentrifugation.

D. Barrick, A. Allgood, 2011, Journal of molecular biology.

Investigations of Heme Protein Absorption Line Shapes, Vibrational Relaxation, and Resonance Raman Scattering on Ultrafast Time Scales †

D. Barrick, D. Ionascu, P. Champion, 2003 .

Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding.

D. Barrick, M. E. Zweifel, 2001, Biochemistry.

The use of consensus sequence information to engineer stability and activity in proteins.

D. Barrick, M. Sternke, K. Tripp, 2020, Methods in enzymology.

Structure and Notch receptor binding of the tandem WWE domain of Deltex.

D. Barrick, D. Leahy, M. E. Zweifel, 2005, Structure.

Stability and cellulolytic activity effects of inse rting endocellulase

D. Barrick, C. Hatem, E. Cunha, 2013 .

Size and sequence and the volume change of protein folding.

D. Barrick, A. Garcia, C. Royer, 2011, Journal of the American Chemical Society.

Quantitative Dissection of the Notch:CSL Interaction: Insights into the Notch Transcriptional Switch

D. Barrick, Raphael Kopan, O. Lubman, 2007 .

Singular value decomposition of protein sequences as a method to visualize sequence and residue space

D. Barrick, Autum R. Baxter‐Koenigs, Gina El Nesr, 2022, Protein science : a publication of the Protein Society.

Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 1. Solution conformational and hydrodynamic properties.

D. Barrick, M. E. Zweifel, 2001, Biochemistry.

Investigations of Anharmonic Low-Frequency Oscillations in Heme Proteins †

D. Barrick, S. Sligar, T. Yonetani, 2002 .

1.46 – Applications of Genetic Engineering

D. Barrick, D. Barrick, 2003 .

The molten globule intermediate of apomyoglobin and the process of protein folding

R. L. Baldwin, D. Barrick, 1993, Protein Science.

Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly.

D. Barrick, Doug Barrick, 1994, Biochemistry.

Three-state analysis of sperm whale apomyoglobin folding.

R. L. Baldwin, D. Barrick, R. Baldwin, 1993, Biochemistry.

Measuring the stability of partly folded proteins using TMAO

Doug Barrick, D. Barrick, Cecilia C Mello, 2003, Protein science : a publication of the Protein Society.

Natural and Designed Enzymes for Cellulose Degradation

D. Barrick, C. Hatem, E. Cunha, 2013 .

Direct NMR Detection of Bifurcated Hydrogen Bonding in the α-Helix N-Caps of Ankyrin Repeat Proteins

D. Barrick, Kevin Sforza, A. Majumdar, 2015, Journal of the American Chemical Society.

The effects of conformational heterogeneity on the binding of the Notch intracellular domain to effector proteins: a case of biologically tuned disorder.

D. Barrick, L. Brand, A. Bertagna, 2008, Biochemical Society transactions.

Structure and stability of the ankyrin domain of the Drosophila Notch receptor

Doug Barrick, D. Barrick, D. Leahy, 2003, Protein science : a publication of the Protein Society.

High-Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine-rich Repeat Protein.

D. Barrick, C. Royer, S. McCallum, 2018, Journal of molecular biology.

Translation initiation in Escherichia coli: sequences within the ribosome‐binding site

G. Stormo, L. Gold, D. Barrick, 1992, Molecular microbiology.

Effect of multiple prolyl isomerization reactions on the stability and folding kinetics of the notch ankyrin domain: experiment and theory.

Doug Barrick, D. Barrick, C. Bradley, 2005, Journal of molecular biology.

Repeat-protein folding: new insights into origins of cooperativity, stability, and topology.

Doug Barrick, Naomi Courtemanche, D. Barrick, 2008, Archives of biochemistry and biophysics.

Enhancing the stability and folding rate of a repeat protein through the addition of consensus repeats.

Doug Barrick, D. Barrick, K. Tripp, 2007, Journal of molecular biology.

The role of introns in repeat protein gene formation.

George D Rose, Doug Barrick, G. Rose, 2006, Journal of molecular biology.

Experimental characterization of the folding kinetics of the notch ankyrin domain.

D. Barrick, C. Bradley, K. Tripp, 2005, Journal of molecular biology.

An improved experimental system for determining small folding entropy changes resulting from proline to alanine substitutions

Doug Barrick, D. Barrick, Timothy O. Street, 2005, Protein science : a publication of the Protein Society.

The tolerance of a modular protein to duplication and deletion of internal repeats.

Doug Barrick, D. Barrick, K. Tripp, 2004, Journal of molecular biology.

Limits of cooperativity in a structurally modular protein: response of the Notch ankyrin domain to analogous alanine substitutions in each repeat.

Doug Barrick, D. Barrick, C. Bradley, 2002, Journal of molecular biology.

Folding landscapes of ankyrin repeat proteins: experiments meet theory.

Elizabeth A Komives, Diego U Ferreiro, Doug Barrick, 2008, Current opinion in structural biology.

Molecular mechanisms of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin.

R. L. Baldwin, D. Barrick, F. Hughson, 1994, Journal of molecular biology.

Distal ligand reactivity and quaternary structure studies of proximally detached hemoglobins.

D. Barrick, V. Simplaceanu, C. Ho, 2001, Biochemistry.

Synergistic enhancement of cellulase pairs linked by consensus ankyrin repeats: Determination of the roles of spacing, orientation, and enzyme identity

D. Barrick, C. Hatem, E. Cunha, 2016, Proteins.

Insertion of Endocellulase Catalytic Domains into Thermostable Consensus Ankyrin Scaffolds: Effects on Stability and Cellulolytic Activity

D. Barrick, C. Hatem, E. Cunha, 2013, Applied and Environmental Microbiology.

Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region.

D. Barrick, A. Bertagna, 2004, Proceedings of the National Academy of Sciences of the United States of America.

A collection of programs for one‐dimensional Ising analysis of linear repeat proteins with point substitutions

D. Barrick, Kathryn Geiger-Schuller, Kevin Sforza, 2020, Protein science : a publication of the Protein Society.

A collection of programs for one-dimensional Ising analysis of linear repeat proteins with point substitutions

D. Barrick, Kathryn Geiger-Schuller, Kevin Sforza, 2020, bioRxiv.

Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape

Doug Barrick, D. Barrick, Timothy O. Street, 2008, Protein science : a publication of the Protein Society.

Thermodynamics, kinetics, and salt dependence of folding of YopM, a large leucine-rich repeat protein.

D. Barrick, E. Kloss, 2008, Journal of molecular biology.

Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curves.

D. Barrick, M. E. Zweifel, 2002, Biophysical chemistry.

Trans‐substitution of the proximal hydrogen bond in myoglobin: II. Energetics, functional consequences, and implications for hemoglobin allostery

D. Barrick, 2000, Proteins.

Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis.

R. L. Baldwin, D. Barrick, F. Hughson, 1991, Biochemistry.

What have we learned from the studies of two-state folders, and what are the unanswered questions about two-state protein folding?

D. Barrick, 2009, Physical biology.

Creating a Homeodomain with High Stability and DNA Binding Affinity by Sequence Averaging.

D. Barrick, A. Majumdar, M. Sternke, 2017, Journal of the American Chemical Society.

Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models.

Doug Barrick, D. Barrick, Tural Aksel, 2009, Methods in enzymology.

FUNCTIONAL CAVITIES IN PROTEINS : A GENERAL METHOD FOR PROXIMAL LIGAND SUBSTITUTION IN MYOGLOBIN

Doug Barrick, S. Boxer, D. Barrick, 1994 .

Nuclear magnetic resonance spectroscopy in the study of hemoglobin cooperativity.

J. Lukin, C. Ho, D. Barrick, 2004, Methods in enzymology.

Histidine 82 influences heme orientational isomerism in sperm whale myoglobin. Long-range effect due to mutation of a conserved residue

Sean V. Taylor, D. Barrick, M. Cocco, 1992 .

The leucine-rich repeat domain of Internalin B folds along a polarized N-terminal pathway.

D. Barrick, N. Courtemanche, 2008, Structure.

A Naturally Occurring Repeat Protein with High Internal Sequence Identity Defines a New Class of TPR-like Proteins.

Doug Barrick, D. Barrick, G. Bowman, 2015, Structure.

The contribution of entropy, enthalpy, and hydrophobic desolvation to cooperativity in repeat-protein folding.

Doug Barrick, D. Barrick, A. Majumdar, 2011, Structure.

Unique features of the folding landscape of a repeat protein revealed by pressure perturbation.

D. Barrick, C. Royer, R. Winter, 2010, Biophysical journal.

The folding of single domain proteins--have we reached a consensus?

Tobin R Sosnick, Doug Barrick, D. Barrick, 2011, Current opinion in structural biology.

Trans‐substitution of the proximal hydrogen bond in myoglobin: I. Structural consequences of hydrogen bond deletion

D. Barrick, Frederick W. Dahlquist, 2000, Proteins.

Structural features of the Notch ankyrin domain-Deltex WWE2 domain heterodimer determined by NMR spectroscopy and functional implications.

D. Barrick, C. Hatem, A. Majumdar, 2023, Structure.

The Notch Transcription Activation Complex Makes Its Move

D. Barrick, Raphael Kopan, 2006, Cell.

A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin

F. Dahlquist, D. Barrick, V. Simplaceanu, 1997, Nature Structural Biology.

The importance of input sequence set to consensus-derived proteins and their relationship to reconstructed ancestral proteins

S. Marqusee, D. Barrick, M. Harms, 2023, bioRxiv.

C‐terminal deletion of leucine‐rich repeats from YopM reveals a heterogeneous distribution of stability in a cooperatively folded protein

D. Barrick, E. Kloss, 2009, Protein science : a publication of the Protein Society.

Effects of Linker Length and Transient Secondary Structure Elements in the Intrinsically Disordered Notch RAM Region on Notch Signaling.

D. Barrick, C. Hatem, A. Majumdar, 2015, Journal of molecular biology.

High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape.

D. Barrick, A. Garcia, C. Roumestand, 2016, Biophysical journal.

A second backbone: the contribution of a buried asparagine ladder to the global and local stability of a leucine-rich repeat protein.

D. Barrick, A. Majumdar, Sean A. Klein, 2019, Biochemistry.

Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor

R. Pappu, D. Barrick, Rahul K. Das, 2017, Proceedings of the National Academy of Sciences.

Predicting coupling limits from an experimentally determined energy landscape

Doug Barrick, D. Barrick, Timothy O. Street, 2007, Proceedings of the National Academy of Sciences.

Stability Islands and the Folding Cooperativity of a Seven-Repeat Array from Topoisomerase V.

D. Barrick, A. Majumdar, Rebecca Fang, 2023, Journal of the American Chemical Society.

Investigations of photolysis and rebinding kinetics in myoglobin using proximal ligand replacements.

Wei Wang, Wenxiang Cao, Xiong Ye, 2004, Biochemistry.

Folding thermodynamics and kinetics of the leucine‐rich repeat domain of the virulence factor Internalin B

D. Barrick, N. Courtemanche, 2008, Protein science : a publication of the Protein Society.

Capping motifs stabilize the leucine‐rich repeat protein PP32 and rigidify adjacent repeats

D. Barrick, A. Majumdar, Thuy P. Dao, 2014, Protein science : a publication of the Protein Society.

Direct observation of parallel folding pathways revealed using a symmetric repeat protein system.

D. Barrick, Tural Aksel, 2014, Biophysical journal.

Broken TALEs: Transcription Activator-like Effectors Populate Partly Folded States.

D. Barrick, Kathryn Geiger-Schuller, Kathryn Geiger-Schuller, 2016, Biophysical journal.

Rerouting the folding pathway of the Notch ankyrin domain by reshaping the energy landscape.

Doug Barrick, D. Barrick, K. Tripp, 2008, Journal of the American Chemical Society.

An experimentally determined protein folding energy landscape.

Doug Barrick, D. Barrick, Cecilia C Mello, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding.

D. Barrick, M. E. Zweifel, 2001, Biochemistry.

The notch ankyrin domain folds via a discrete, centralized pathway.

Doug Barrick, D. Barrick, C. Bradley, 2006, Structure.

Analysis of Tandem Repeat Protein Folding Using Nearest-Neighbor Models.

D. Barrick, Mark Petersen, 2021, Annual Review of Biophysics.

Quantitative analysis of ribosome binding sites in E.coli.

T. D. Schneider, G. Stormo, L. Gold, 1994, Nucleic acids research.

Deletion of internal structured repeats increases the stability of a leucine-rich repeat protein, YopM.

D. Barrick, Ellen F. Vieux, 2011, Biophysical chemistry.

Functional instability allows access to DNA in longer transcription Activator-Like effector (TALE) arrays

D. Barrick, T. Ha, Kathryn Geiger-Schuller, 2019, eLife.

Functional instability allows access to DNA in longer Transcription Activator-Like Effector (TALE) arrays

D. Barrick, Kathryn Geiger-Schuller, Jaba Mitra, 2018, bioRxiv.

Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor

R. Pappu, D. Barrick, Rahul K. Das, 2017, Proceedings of the National Academy of Sciences.

Thermodynamic Analysis of the CSL·Notch Interaction

D. Barrick, Raphael Kopan, M. Ilagan, 2009, The Journal of Biological Chemistry.

C‐terminal deletion of leucine‐rich repeats from YopM reveals a heterogeneous distribution of stability in a cooperatively folded protein

D. Barrick, E. Kloss, 2009, Protein science : a publication of the Protein Society.

Size and sequence and the volume change of protein folding.

D. Barrick, A. Garcia, C. Royer, 2011, Journal of the American Chemical Society.

Irreversible assembly of membrane fusion machines

D. Barrick, F. Hughson, 2002, Nature Structural Biology.

The Second Law and Entropy

D. Barrick, 2017 .