D. W. Bolen

发表

Structure and energetics of the hydrogen-bonded backbone in protein folding.

G. Rose, D. W. Bolen, George D Rose, 2008, Annual review of biochemistry.

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants.

D. W. Bolen, M. Santoro, M. Santoro, 1988, Biochemistry.

Backbone additivity in the transfer model of protein solvation

Gillian C. Lynch, H. Kokubo, B. Pettitt, 2010, Protein science : a publication of the Protein Society.

Predicting the energetics of osmolyte-induced protein folding/unfolding.

D. W. Bolen, M. Auton, 2005, Proceedings of the National Academy of Sciences of the United States of America.

A molecular mechanism for osmolyte-induced protein stability

G. Rose, D. W. Bolen, Timothy O. Street, 2006, Proceedings of the National Academy of Sciences.

Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins

V. Hilser, T. Schrank, D. W. Bolen, 2009, Proceedings of the National Academy of Sciences.

Molecular basis of the apparent near ideality of urea solutions.

B Montgomery Pettitt, Hironori Kokubo, H. Kokubo, 2007, Biophysical journal.

Hydrogen exchange kinetics of RNase A and the urea:TMAO paradigm.

D. W. Bolen, Y. Qu, 2003, Biochemistry.

Erratum: A molecular mechanism for osmolyte-induced protein stability (Proceedings of the National Academy of Sciences of the United States of America (September 19, 2006) 38, 103 (13997-14002) DOI 10.1073/pnas.0606236103)

G. Rose, D. W. Bolen, Timothy O. Street, 2006 .

Osmolyte‐induced conformational changes in the Hsp90 molecular chaperone

D. Agard, D. W. Bolen, K. Krukenberg, 2009, Protein science : a publication of the Protein Society.

A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation.

D. W. Bolen, A. Wang, A. Wang, 1997, Biochemistry.

A guanidine hydrochloride induced change in ribonuclease without gross unfolding.

D. W. Bolen, J. F. Miller, 1978, Biochemical and biophysical research communications.

Effects of cell volume regulating osmolytes on glycerol 3-phosphate binding to triosephosphate isomerase.

Linlin Qiu, R. Callender, D. W. Bolen, 2007, Biochemistry.

Protein phase diagrams II: nonideal behavior of biochemical reactions in the presence of osmolytes.

J. Ferreon, A. C. Ferreon, D. W. Bolen, 2007, Biophysical journal.

Uncovering the basis for nonideal behavior of biological molecules.

B. Pettitt, D. W. Bolen, J. Rösgen, 2004, Biochemistry.

Calorimetric determination of the enthalpy change for the a-helix to coil transition of an alanine peptide in water ( L-alanine helix / peptide hydrogen bond / helix-coil enthalpy )

R. L. Baldwin, S. Marqusee, J. M. Scholtz, 2022 .

Calorimetric studies of protein--inhibitor interaction. I. Binding of 3'-cytidine monophosphate to ribonuclease A at pH 5.5.

D. W. Bolen, R. Biltonen, M. Flögel, 1971, Biochemistry.

Naturally Occurring ( Protecting and Nonprotecting )

D. W. Bolen, Osmolytes, 2017 .

Thermodynamics of zinc binding to rhodanese.

D. W. Bolen, S. Rajender, 1974, Archives of biochemistry and biophysics.

Increased thermal stability of proteins in the presence of naturally occurring osmolytes.

D. W. Bolen, Y. Liu, M. Santoro, 1992, Biochemistry.

Calorimetric determination of linkage effects involving an acyl-enzyme intermediate.

D. W. Bolen, J. Slightom, 1990, Biophysical chemistry.

Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis.

I. Baskakov, D. W. Bolen, A. Wang, 1998, Biophysical journal.

An analysis of the molecular origin of osmolyte‐dependent protein stability

B. Pettitt, D. W. Bolen, J. Rösgen, 2007, Protein science : a publication of the Protein Society.

Protein folding, stability, and solvation structure in osmolyte solutions.

B. Pettitt, D. W. Bolen, J. Rösgen, 2005, Biophysical journal.

The osmophobic effect: natural selection of a thermodynamic force in protein folding.

I. Baskakov, D. W. Bolen, D.W Bolen, 2001, Journal of molecular biology.

Osmolyte-driven contraction of a random coil protein.

D. W. Bolen, Y. Qu, C. Bolen, 1998, Proceedings of the National Academy of Sciences of the United States of America.

The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes.

D. W. Bolen, Y. Liu, Yufeng Liu, 1995, Biochemistry.

Effect of proline on lactate dehydrogenase activity: testing the generality and scope of the compatibility paradigm.

D. W. Bolen, A. Wang, A. Wang, 1996, Biophysical journal.

The Conformation of the Glucocorticoid Receptor AF1/tau1 Domain Induced by Osmolyte Binds Co-regulatory Proteins*

J. Lee, Raj Kumar, D. W. Bolen, 2001, The Journal of Biological Chemistry.

Trimethylamine N-Oxide-induced Cooperative Folding of an Intrinsically Unfolded Transcription-activating Fragment of Human Glucocorticoid Receptor*

I. Baskakov, Raj Kumar, D. W. Bolen, 1999, The Journal of Biological Chemistry.

Time-dependent effects of trimethylamine-N-oxide/urea on lactate dehydrogenase activity: an unexplored dimension of the adaptation paradigm.

I. Baskakov, D. W. Bolen, 1998, Biophysical journal.

Forcing Thermodynamically Unfolded Proteins to Fold*

I. Baskakov, D. W. Bolen, 1998, The Journal of Biological Chemistry.

Structural Stability of Rhodopsin and Opsin Studied by Differential Scanning Calorimetry

D. W. Bolen, P. Hargrave, M. Santoro, 1992 .

Kinetic properties of adenosine deaminase in mixed aqueous solvents.

D. W. Bolen, J. Fisher, 1969, Biochemistry.

Interdomain Signaling in a Two-domain Fragment of the Human Glucocorticoid Receptor*

J. Lee, I. Baskakov, Raj Kumar, 1999, The Journal of Biological Chemistry.

Additive transfer free energies of the peptide backbone unit that are independent of the model compound and the choice of concentration scale.

D. W. Bolen, M. Auton, 2004, Biochemistry.

A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range.

M M Santoro, D. W. Bolen, M. Santoro, 1992, Biochemistry.

Osmolyte effects on kinetics of FKBP12 C22A folding coupled with prolyl isomerization.

Andrew T. Russo, D. W. Bolen, J. Rösgen, 2003, Journal of molecular biology.

Protein stabilization by naturally occurring osmolytes.

D. W. Bolen, D. Bolen, 2001, Methods in molecular biology.

[2] Probes of energy transduction in enzyme catalysis

D. W. Bolen, Yingwen Huang, 1995 .

Covalent bond changes as a driving force in enzyme catalysis.

D. W. Bolen, Y. Huang, Yingwen Huang, 1993, Biochemistry.

Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of delta G degrees N-U values in a thermodynamic cycle.

D. W. Bolen, M. Santoro, M. Santoro, 1988, Biochemistry.

Stereochemical and kinetic studies on the action of the catalytic subunit of bovine cardiac muscle adenosine 3',5'-monophosphate dependent protein kinase using metal ion complexes of ATP beta S.

D. W. Bolen, E. Kaiser, H. N. Bramson, 1980, Biochemistry.

Hydrolysis enthalpy changes for selected five- and six-membered cyclic esters

D. W. Bolen, E. Izbicka, 1978 .

The paradox between m values and δCp' for denaturation of ribonuclease T1 with disulfide bonds intact and broken

I. Baskakov, D. W. Bolen, 1999, Protein science : a publication of the Protein Society.

Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease A.

A. D. Robertson, D. W. Bolen, A. Wang, 1995, Biochemistry.

Structural thermodynamics of protein preferential solvation: Osmolyte solvation of proteins, aminoacids, and peptides

D. W. Bolen, M. Auton, J. Rösgen, 2008, Proteins.

Osmolyte effects on protein stability and solubility: a balancing act between backbone and side-chains.

D. W. Bolen, M. Auton, J. Rösgen, 2011, Biophysical chemistry.

The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry

R. L. Baldwin, S. Loh, D. W. Bolen, 2000, Protein science : a publication of the Protein Society.

Synthesis, purification, and characterization of the A and B diastereomers of gamma-32P-labeled adenosine 5'-O-(2-thiotriphosphate).

D. W. Bolen, E. Kaiser, J. Stingelin, 1980, The Journal of biological chemistry.

How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability.

M. Yao, D. W. Bolen, Min Yao, 1995, Biochemistry.

Application of the transfer model to understand how naturally occurring osmolytes affect protein stability.

D. W. Bolen, M. Auton, 2007, Methods in enzymology.

Mixed osmolytes: The degree to which one osmolyte affects the protein stabilizing ability of another

D. W. Bolen, Luis Marcelo F Holthauzen, D Wayne Bolen, 2006, Protein science : a publication of the Protein Society.

Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water.

R. L. Baldwin, S. Marqusee, J. M. Scholtz, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Effects of naturally occurring osmolytes on protein stability and solubility: issues important in protein crystallization.

D. W. Bolen, 2004, Methods.

Energetics of alpha-chymotrypsin-mediated hydrolysis of a strained cyclic ester.

D. W. Bolen, T. Kimura, Y. Nitta, 1987, Biochemistry.

Anatomy of energetic changes accompanying urea-induced protein denaturation

D. W. Bolen, M. Auton, L. M. Holthauzen, 2007, Proceedings of the National Academy of Sciences.

Hydrogen Bonding Progressively Strengthens upon Transfer of the Protein Urea-Denatured State to Water and Protecting Osmolytes†

D. W. Bolen, J. Rösgen, L. M. Holthauzen, 2010, Biochemistry.

Enthalpy changes accompanying hydrolysis of 3-(2-furyl)acryloylimidazole by .alpha.-chymotrypsin

D. W. Bolen, J. Slightom, 1980 .

Thermal behavior of HeLa and KB cells in suspension and attached to glass.

D. W. Bolen, D. Cerretti, J. Dorsey, 1977, Biochimica et biophysica acta.

Monitoring the sizes of denatured ensembles of staphylococcal nuclease proteins: implications regarding m values, intermediates, and thermodynamics.

I. Baskakov, D. W. Bolen, 1998, Biochemistry.

Effects of guanidine hydrochloride on the proton inventory of proteins: implications on interpretations of protein stability.

D. W. Bolen, M. Yang, 2000, Biochemistry.

Osmolyte‐induced protein folding free energy changes

D. W. Bolen, Peng Wu, 2006, Proteins.

Thermodynamics of denaturant-induced unfolding of a protein that exhibits variable two-state denaturation.

A. C. Ferreon, D. W. Bolen, 2004, Biochemistry.

Structural thermodynamics of a random coil protein in guanidine hydrochloride

A. C. Ferreon, D. W. Bolen, M. Yang, 2000, Proteins.

Metrics that differentiate the origins of osmolyte effects on protein stability: a test of the surface tension proposal.

A. C. Ferreon, D. W. Bolen, M. Auton, 2006, Journal of molecular biology.

Efficacy of macromolecular crowding in forcing proteins to fold.

D. W. Bolen, Y. Qu, 2002, Biophysical chemistry.

preferential solvation: Osmolyte solvation of proteins, aminoacids, and peptides

D. W. Bolen, M. Auton, J. Rösgen, 2008 .

Statistical Thermodynamic Approach to the Chemical Activities in Two-Component Solutions

B. Pettitt, D. W. Bolen, J. Rösgen, 2004 .

Interactions of five- and six-membered cyclic esters with α-chymotrypsin: Kinetic evidence for covalent enzyme intermediates

D. W. Bolen, E. Izbicka, 1981 .

Isolation and partial characterization of a covalent intermediate between α-chymotrypsin and o-hydroxy-α-toluenesulfonic acid sultone

D. W. Bolen, E. Izbicka, 1981 .