Robert Baldwin

About

Robert "Buzz" Baldwin is an Emeritus Faculty member in the Stanford Biochemistry Department. His professional biography on the Stanford webpage includes a detailed list of his students and postdoctoral fellows spanning from the 1960s through the 2000s, indicating a long-standing career in biochemistry research and mentorship. The page does not provide specific information about his research focus, background, or key contributions, but his extensive mentorship history suggests a significant role in advancing biochemistry education and research at Stanford.

Research topics

• Chemistry
• Crystallography
• Stereochemistry
• Biophysics
• Computer science

Selected publications

• Molten globules, entropy-driven conformational change and protein folding

  Current Opinion in Structural Biology · 2012-12-10 · 130 citations

  review1st authorCorresponding
  PublisherDOI

• Dry molten globule intermediates and the mechanism of protein unfolding

  Proteins Structure Function and Bioinformatics · 2010-06-15 · 115 citations

  articleOpen access1st authorCorresponding

  New experimental results show that either gain or loss of close packing can be observed as a discrete step in protein folding or unfolding reactions. This finding poses a significant challenge to the conventional two-state model of protein folding. Results of interest involve dry molten globule (DMG) intermediates, an expanded form of the protein that lacks appreciable solvent. When an unfolding protein expands to the DMG state, side chains unlock and gain conformational entropy, while liquid-li…

  PublisherOA PDFDOI

• Populations of the three major backbone conformations in 19 amino acid dipeptides

  Proceedings of the National Academy of Sciences · 2011-01-04 · 114 citations

  articleOpen access

  The amide III region of the peptide infrared and Raman spectra has been used to determine the relative populations of the three major backbone conformations (P(II), β, and α(R)) in 19 amino acid dipeptides. The results provide a benchmark for force field or other methods of predicting backbone conformations in flexible peptides. There are three resolvable backbone bands in the amide III region. The major population is either P(II) or β for all dipeptides except Gly, whereas the α(R) population i…

  PublisherOA PDFDOI

• How the hydrophobic factor drives protein folding

  Proceedings of the National Academy of Sciences · 2016-10-17 · 102 citations

  articleOpen access1st authorCorresponding

  How hydrophobicity (HY) drives protein folding is studied. The 1971 Nozaki-Tanford method of measuring HY is modified to use gases as solutes, not crystals, and this makes the method easy to use. Alkanes are found to be much more hydrophobic than rare gases, and the two different kinds of HY are termed intrinsic (rare gases) and extrinsic (alkanes). The HY values of rare gases are proportional to solvent-accessible surface area (ASA), whereas the HY values of alkanes depend on special hydration…

  PublisherOA PDFDOI

• Dynamic hydration shell restores Kauzmann's 1959 explanation of how the hydrophobic factor drives protein folding

  Proceedings of the National Academy of Sciences · 2014-08-25 · 102 citations

  articleOpen access1st authorCorresponding

  Kauzmann's explanation of how the hydrophobic factor drives protein folding is reexamined. His explanation said that hydrocarbon hydration shells are formed, possibly of clathrate water, and they explain why hydrocarbons have uniquely low solubilities in water. His explanation was not universally accepted because of skepticism about the clathrate hydration shell. A revised version is given here in which a dynamic hydration shell is formed by van der Waals (vdw) attraction, as proposed in 1985 by…

  PublisherOA PDFDOI

Recent grants

• NIH Grant R37GM019988

  NIH · $3.2M · 1999

• NIH Grant R01GM019988

  NIH · $848k · 1988

• NIH Grant R01GM031475

  NIH · $2.2M · 1998

Frequent coauthors

• Der‐Hang Chin

  National Chung Hsing University

  41 shared

• Franc Avbelj

  National Institute of Chemistry

  40 shared

• Peter S. Kim

  Chan Zuckerberg Initiative (United States)

  38 shared

• Carol A. Rohl

  Institute of Informatics of the Slovak Academy of Sciences

  36 shared

• Eunice J. York

  Columbia University

  27 shared

• Kevin Shoemaker

  27 shared

• Robert Fairman

  26 shared

• Robert W. Woody

  Colorado State University

  25 shared

Labs

• Robert Baldwin LabPI

Similar researchers at Stanford University

• Arthur Kornbergh-114
• Paul Bergh-112
• Chaitan Khoslah-110