Robert L. Baldwin
Active 1952–2019
- 120
- Papers
- 29,494
- Citations
- 99
- h-index
- 120
- i10-index
Citations
Citation sources
Countries
Institutions
Fields
- Biochemistry, Genetics and Molecular Biology68.5%
- Medicine7.4%
- Materials Science4.9%
- Chemistry4.7%
- Physics and Astronomy2.6%
- Immunology and Microbiology2.6%
- Other9.3%
Topics
- Protein Structure and Dynamics15.2%
- Enzyme Structure and Function9.4%
- RNA and protein synthesis mechanisms6.1%
- DNA and Nucleic Acid Chemistry5.1%
- Chemical Synthesis and Analysis2.8%
- Mass Spectrometry Techniques and Applications2.5%
- Other58.9%
Coauthors
- Eunice J. York10
- J. Martin Scholtz9
- Avijit Chakrabartty7
- Carol A. Rohl7
- George D. Rose6
- John M. Stewart6
- Peter S. Kim6
- Doug Barrick5
- Franc Avbelj5
- S. Padmanabhan5
- Susan Marqusee5
- Frederick M. Hughson4
- Kevin Shoemaker4
- Andrew J. Doig3
- Beatrice M.P. Huyghues‐Despointes3
- Elliot L. Elson3
- Franz X. Schmid3
- J M Stewart3
- Peizhi Luo3
- Robert Fairman3
- Andrew D. Robertson2
- Barry T. Nall2
- David Shore2
- Der‐Hang Chin2
All papers
- How Hofmeister ion interactions affect protein stability
Authors: Robert L. Baldwin - Biophysical Journal 1996 cited by 1,133
- Temperature dependence of the hydrophobic interaction in protein folding.
Authors: Robert L. Baldwin - National Academy of Sciences, Proceedings of the National Academy of Sciences 1986 cited by 899
- Mechanism of Helix Induction by Trifluoroethanol: A Framework for Extrapolating the Helix-Forming Properties of Peptides from Trifluoroethanol/Water Mixtures Back to Water
Authors: Peizhi Luo, Robert L. Baldwin - Biochemistry 1997 cited by 653
- Energetics of Protein Folding
Authors: Robert L. Baldwin - Journal of Molecular Biology 2007 cited by 303
- N‐ and C‐capping preferences for all 20 amino acids in α‐helical peptides
Authors: Andrew J. Doig, Robert L. Baldwin - Protein Science 1995 cited by 324
- Unusually stable helix formation in short alanine-based peptides.
Authors: Susan Marqusee, Virginia H. Robbins, Robert L. Baldwin - National Academy of Sciences, Proceedings of the National Academy of Sciences 1989 cited by 776
- Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactions
Authors: Avijit Chakrabartty, Tanja Kortemme, Robert L. Baldwin - Protein Science 1994 cited by 620
- Cation-induced toroidal condensation of DNA
Authors: Jonathan Widom, Robert L. Baldwin - Journal of Molecular Biology 1980 cited by 548
- How the hydrophobic factor drives protein folding
Authors: Robert L. Baldwin, George D. Rose - National Academy of Sciences, Proceedings of the National Academy of Sciences 2016 cited by 103
- Parameters of helix–coil transition theory for alanine‐based peptides of varying chain lengths in water
Authors: J. Martin Scholtz, Hong Qian, Eunice J. York, John M. Stewart, Robert L. Baldwin - Biopolymers 1991 cited by 502
- Polyproline II structure in a sequence of seven alanine residues
Authors: Zhengshuang Shi, C. Anders Olson, George D. Rose, Robert L. Baldwin, Neville R. Kallenbach - National Academy of Sciences, Proceedings of the National Academy of Sciences 2002 cited by 476
- Relative helix-forming tendencies of nonpolar amino acids
Authors: S. Padmanabhan, Susan Marqusee, Theresa M. Ridgeway, Thomas M. Laue, Robert L. Baldwin - Nature 1990 cited by 458
- Monomolecular condensation of λ‐DNA induced by cobalt hexammine
Authors: Jonathan Widom, Robert L. Baldwin - Biopolymers 1983 cited by 208
- Molten globules, entropy-driven conformational change and protein folding
Authors: Robert L. Baldwin, George D. Rose - Current Opinion in Structural Biology 2012 cited by 130
- Dry molten globule intermediates and the mechanism of protein unfolding
Authors: Robert L. Baldwin, Carl Frieden, George D. Rose - Proteins Structure Function and Bioinformatics 2010 cited by 115
- Dynamic hydration shell restores Kauzmann's 1959 explanation of how the hydrophobic factor drives protein folding
Authors: Robert L. Baldwin - National Academy of Sciences, Proceedings of the National Academy of Sciences 2014 cited by 102
- Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design.
Authors: Susan Marqusee, Robert L. Baldwin - National Academy of Sciences, Proceedings of the National Academy of Sciences 1987 cited by 956
- Tests of the helix dipole model for stabilization of α-helices
Authors: Kevin Shoemaker, Peter S. Kim, Eunice J. York, John M. Stewart, Robert L. Baldwin - Nature 1987 cited by 603
- Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities
Authors: Avijit Chakrabartty, Tanja Kortemme, S. Padmanabhan, Robert L. Baldwin - Biochemistry 1993 cited by 306
- Deprivation-induced cortical reorganization in children with cochlear implants
Authors: Anu Sharma, Phillip M. Gilley, Michael F. Dorman, Robert L. Baldwin - International Journal of Audiology 2007 cited by 253
- [1] Deciphering rules of helix stability in peptides
Authors: Carol A. Rohl, Robert L. Baldwin - Methods in enzymology on CD-ROM/Methods in enzymology 1998 cited by 127
- Intrinsic backbone preferences are fully present in blocked amino acids
Authors: Franc Avbelj, Simona Golič Grdadolnik, Jože Grdadolnik, Robert L. Baldwin - National Academy of Sciences, Proceedings of the National Academy of Sciences 2006 cited by 124
- Charged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone charges.
Authors: Katherine M. Armstrong, Robert L. Baldwin - National Academy of Sciences, Proceedings of the National Academy of Sciences 1993 cited by 110
- The enthalpy of the alanine peptide helix measured by isothermal titration calorimetry using metal-binding to induce helix formation
Authors: María M. López, Der‐Hang Chin, Robert L. Baldwin, George I. Makhatadze - National Academy of Sciences, Proceedings of the National Academy of Sciences 2002 cited by 105
