Stephen H. White

ORCID: 0000-0001-8540-7907
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About
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Research Areas
  • Lipid Membrane Structure and Behavior
  • Protein Structure and Dynamics
  • RNA and protein synthesis mechanisms
  • Bacterial Genetics and Biotechnology
  • Spectroscopy and Quantum Chemical Studies
  • Total Knee Arthroplasty Outcomes
  • Orthopaedic implants and arthroplasty
  • Ion channel regulation and function
  • Antimicrobial Peptides and Activities
  • Knee injuries and reconstruction techniques
  • Enzyme Structure and Function
  • RNA Interference and Gene Delivery
  • Nanopore and Nanochannel Transport Studies
  • Bacteriophages and microbial interactions
  • Supramolecular Self-Assembly in Materials
  • Metabolomics and Mass Spectrometry Studies
  • Photoreceptor and optogenetics research
  • Electrochemical Analysis and Applications
  • Surfactants and Colloidal Systems
  • Photosynthetic Processes and Mechanisms
  • Machine Learning in Bioinformatics
  • Force Microscopy Techniques and Applications
  • Advanced biosensing and bioanalysis techniques
  • Neuroscience and Neuropharmacology Research
  • Neuroscience and Neural Engineering

University of California, Irvine
2013-2023

National Institute of Standards and Technology
2009-2023

NIST Center for Neutron Research
2009-2023

Robert Jones and Agnes Hunt Orthopaedic Hospital
2001-2018

Nuffield Health
2018

UC Irvine Health
2010-2018

Suffolk University
2012

Interface (United States)
2005-2011

University of California System
1984-2010

Stockholm University
2005

One of the ubiquitous features membrane proteins is preference tryptophan and tyrosine residues for surfaces that presumably arises from enhanced stability due to distinct interfacial interactions. The physical basis this widely believed arise amphipathic interactions related imino group hydrogen bonding and/or dipole We have examined these other possibilities tryptophan's by using 1H magic angle spinning (MAS) chemical shift measurements, two-dimensional (2D) nuclear Overhauser effect...

10.1021/bi980809c article EN Biochemistry 1998-10-01

Octanol-to-water solvation free energies of acetyl amino acid amides (Ac-X-amides) [Fauchère, J. L., & Pliška, V. (1983) Eur. Med. Chem.Chim. Ther. 18, 369] form the basis for computational comparisons protein stabilities by means atomic parameter formalism Eisenberg and McLachlan [(1986) Nature 319, 199]. In order to explore this approach more complex systems, we have determined octanol-to-water partitioning (1) guest (X) side chains in host−guest pentapeptides AcWL-X-LL, (2) carboxy...

10.1021/bi9600153 article EN Biochemistry 1996-01-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThe nature of the hydrophobic binding small peptides at bilayer interface: implications for insertion transbilayer helicesRussell E. Jacobs and Stephen H. WhiteCite this: Biochemistry 1989, 28, 8, 3421–3437Publication Date (Print):April 18, 1989Publication History Published online1 May 2002Published inissue 18 April 1989https://pubs.acs.org/doi/10.1021/bi00434a042https://doi.org/10.1021/bi00434a042research-articleACS PublicationsRequest reuse...

10.1021/bi00434a042 article EN Biochemistry 1989-04-01

Abstract Lipids are produced, transported, and recognized by the concerted actions of numerous enzymes, binding proteins, receptors. A comprehensive analysis lipid molecules, “lipidomics,” in context genomics proteomics is crucial to understanding cellular physiology pathology; consequently, biology has become a major research target postgenomic revolution systems biology. To facilitate international communication about lipids, classification lipids with common platform that compatible...

10.1002/ejlt.200405001 article EN European Journal of Lipid Science and Technology 2005-05-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructure of lamellar lipid domains and corneocyte envelopes murine stratum corneum. An x-ray diffraction studyStephen H. White, Dorla Mirejovsky, Glen I. KingCite this: Biochemistry 1988, 27, 10, 3725–3732Publication Date (Print):May 1, 1988Publication History Published online1 May 2002Published inissue 1 1988https://pubs.acs.org/doi/10.1021/bi00410a031https://doi.org/10.1021/bi00410a031research-articleACS PublicationsRequest reuse...

10.1021/bi00410a031 article EN Biochemistry 1988-05-01

Defensins comprise a family of broad-spectrum antimicrobial peptides that are stored in the cytoplasmic granules mammalian neutrophils and Paneth cells small intestine. Neutrophil defensins known to permeabilize cell membranes susceptible microorganisms, but mechanism permeabilization is uncertain. We report here results an investigation by which HNP-2, one 4 human neutrophil defensins, permeabilizes large unilamellar vesicles formed from anionic lipid palmitoyloleoylphosphatidylglycerol...

10.1002/pro.5560030902 article EN Protein Science 1994-09-01

The rate of membrane protein (MP) structure determination has been examined for the 18-year period following publication first high-resolution crystal structure. growth is solidly exponential, but lags behind soluble proteins during equivalent time period.

10.1110/ps.04712004 article EN Protein Science 2004-06-23

Hydropathy plot methods form a cornerstone of membrane protein research, especially in the early stages biochemical and structural characterization. Membrane Protein Explorer (MPEx), described this article, is refined versatile hydropathy-plot software tool for analyzing sequences. MPEx highly interactive facilitates characterization identification favorable transmembrane regions using experiment-based physical biological hydrophobicity scales. Besides allowing consequences sequence...

10.1002/pro.256 article EN Protein Science 2009-09-25

10.1016/s0005-2736(01)00382-0 article EN publisher-specific-oa Biochimica et Biophysica Acta (BBA) - Biomembranes 2001-10-01
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