David E. Wemmer

About

David E. Wemmer, born in 1951, is a Professor of the Graduate School and Emeritus Professor of Chemistry at the University of California, Berkeley. He holds a B.S. degree from the University of California, Davis, obtained in 1973, and a Ph.D. in Physical Chemistry from UC Berkeley, earned in 1979. His professional experience includes serving as Operations Manager of the NIH NMR Facility at Stanford University from 1980 to 1982 and as a Research Assistant Professor at the University of Washington from 1983 to 1985. Professor Wemmer's research focuses on biophysical chemistry, specifically investigating proteins, nucleic acids, and their interactions using NMR spectroscopy. His laboratory aims to understand the interactions that govern the function of biopolymers such as proteins, DNA, and RNA, including conformational stability and molecular interactions essential for biological activity. His work employs nuclear magnetic resonance, particularly multidimensional methods with biosynthetic isotope enrichment, to determine solution structures, analyze conformational fluctuations, and study complex formation. His research has contributed to understanding DNA-ligand interactions, especially in recognizing sequence-specific binding of small molecules to DNA, and exploring the structural and functional aspects of regulatory proteins involved in genetic expression, including transcription factors and RNA-binding proteins.

Research topics

• Chemistry
• Stereochemistry
• Crystallography
• Biology
• Biochemistry

Selected publications

• Finding Our Way in the Dark Proteome

  Journal of the American Chemical Society · 2016-07-07 · 130 citations

  articleOpen access

  The traditional structure-function paradigm has provided significant insights for well-folded proteins in which structures can be easily and rapidly revealed by X-ray crystallography beamlines. However, approximately one-third of the human proteome is comprised of intrinsically disordered proteins and regions (IDPs/IDRs) that do not adopt a dominant well-folded structure, and therefore remain "unseen" by traditional structural biology methods. This Perspective considers the challenges raised by…

  PublisherOA PDFDOI

• Fragmentation of Lignin Samples with Commercial Pd/C under Ambient Pressure of Hydrogen

  ACS Catalysis · 2016-09-19 · 106 citations

  article

  We report the reagentless cleavage of prevalent β-O-4 linkages in lignin model compounds, as well as the cleavage of several types of organosolv lignins, catalyzed by commercially available Pd/C. Such lignin fragmentation occurred without added reagent if the indigenous double bonds were reduced first or it occurred under conditions in which just 1 atm of hydrogen was added to the system to reduce C═C bonds of the original lignin sample in situ prior to fragmentation. A detailed view of the site…

  PublisherDOI

• Cellulose Deficiency Is Enhanced on Hyper Accumulation of Sucrose by a H⁺-Coupled Sucrose Symporter

  PLANT PHYSIOLOGY · 2016-03-24 · 53 citations

  articleOpen access

  In order to understand factors controlling the synthesis and deposition of cellulose, we have studied the Arabidopsis (Arabidopsis thaliana) double mutant shaven3 shaven3-like1 (shv3svl1), which was shown previously to exhibit a marked cellulose deficiency. We discovered that exogenous sucrose (Suc) in growth medium greatly enhances the reduction in hypocotyl elongation and cellulose content of shv3svl1 This effect was specific to Suc and was not observed with other sugars or osmoticum. Live-cel…

  PublisherOA PDFDOI

• Rotaxane-mediated suppression and activation of cucurbit[6]uril for molecular detection by ¹²⁹Xe hyperCEST NMR

  Chemical Communications · 2016-01-01 · 51 citations

  article

  We report a method for blocking interactions between (129)Xe and cucurbit[6]uril (CB6) until activation by a specific chemical event. We synthesized a CB6-rotaxane that allowed no (129)Xe interaction with the CB6 macrocycle component until a cleavage event released the CB6, which then produced a (129)Xe@CB6 NMR signal. This contrast-upon-activation (129)Xe NMR platform allows for modular synthesis and can be expanded to applications in detection and disease imaging.

  PublisherDOI

• Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR

  Biochemistry · 2016-03-21 · 44 citations

  articleOpen accessSenior author

  Elucidation of structural changes involved in protein misfolding and amyloid formation is crucial for unraveling the molecular basis of amyloid formation. Here we report structural analyses of the amyloidogenic intermediate and amyloid aggregates of transthyretin using solution and solid-state nuclear magnetic resonance (NMR) spectroscopy. Our solution NMR results show that one of the two main β-sheet structures (CBEF β-sheet) is maintained in the aggregation-competent intermediate, while the ot…

  PublisherOA PDFDOI

Recent grants

• NIH Grant S10RR015756

  NIH · $500k · 2002

• Molecular Biophysics Training Grant

  NIH · $9.6M · 1989–2023

• NIH Grant R01GM062163

  NIH · $3.1M · 2016

Frequent coauthors

• Alexander Pines

  University of California, Berkeley

  263 shared

• Jeffrey G. Pelton

  QB3

  126 shared

• Thomas J. Lowery

  89 shared

• John Kuriyan

  Vanderbilt University

  80 shared

• Eliseo Ruíz

  Universitat de Barcelona

  76 shared

• Matthew B. Francis

  University of California, Berkeley

  65 shared

• Peter G. Schultz

  Scripps Research Institute

  63 shared

• Seth M. Rubin

  University of California, Santa Cruz

  53 shared

Education

• Ph.D., Chemistry

  University of California Berkeley

  1979

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• Jeffrey R. Longh-189