Dr. David F. Green MD
Urologist
250 Pleasant St Concord NH, 03301About
Dr. David Green is a urologist practicing in Concord, NH. Dr. Green specializes in diseases of the urinary tract and the male reproductive system. This includes areas of the bladder, urethra, kidneys, penis and prostate. Urology is a surgical specialty and requires knowledge in other areas of expertise such as gynecology and internal medicine due to the variety of clinical problems that are involved.
Education and Training
Pa State Univ Coll Of Med- Hershey Pa 1979
Pennsylvania State University College of Medicine 1975
Board Certification
UrologyAmerican Board of UrologyABU
Provider Details
Expert Publications
Data provided by the National Library of Medicine- X-ray structural and simulation analysis of a protein mutant: the value of a combined approach.
- Escherichia coli glutaminyl-tRNA synthetase is electrostatically optimized for binding of its cognate substrates.
- Action-at-a-distance interactions enhance protein binding affinity.
- Design of improved protein inhibitors of HIV-1 cell entry: Optimization of electrostatic interactions at the binding interface.
- Rational design of new binding specificity by simultaneous mutagenesis of calmodulin and a target peptide.
- Optimized parameters for continuum solvation calculations with carbohydrates.
- Evaluation of electrostatic interactions.
- Computational models explain the oligosaccharide specificity of cyanovirin-N.
- Interpretation of p-cyanophenylalanine fluorescence in proteins in terms of solvent exposure and contribution of side-chain quenchers: a combined fluorescence, IR and molecular dynamics study.
- Energetic decomposition with the generalized-born and Poisson-Boltzmann solvent models: lessons from association of G-protein components.
- Rational and computational design of stabilized variants of cyanovirin-N that retain affinity and specificity for glycan ligands.
- Biophysical and functional analyses suggest that adenovirus E4-ORF3 protein requires higher-order multimerization to function against promyelocytic leukemia protein nuclear bodies.
- Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects.
- Carbohydrate recognition by the antiviral lectin cyanovirin-N.
- Rational modification of protein stability by targeting surface sites leads to complicated results.
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