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  1. Article ; Online: One sequence plus one mutation equals two folds.

    Shortle, David

    Proceedings of the National Academy of Sciences of the United States of America

    2009  Volume 106, Issue 50, Page(s) 21011–21012

    MeSH term(s) Amino Acid Sequence ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Point Mutation ; Protein Conformation ; Protein Folding ; Streptococcus/chemistry
    Chemical Substances Bacterial Proteins ; IgG Fc-binding protein, Streptococcus ; Peptide Fragments
    Language English
    Publishing date 2009-12-08
    Publishing country United States
    Document type Comment ; Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.0912370107
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
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  2. Article ; Online: Addressing the spatial disconnect between national-scale total maximum daily loads and localized land management decisions.

    Amin, M G Mostofa / Veith, Tamie L / Shortle, James S / Karsten, Heather D / Kleinman, Peter J A

    Journal of environmental quality

    2020  Volume 49, Issue 3, Page(s) 613–627

    Abstract: Regulatory watershed mitigation programs typically emphasize widespread adoption of best management practices (BMPs) to meet total maximum daily load (TMDL) goals. To comply with the Chesapeake Bay TMDL, jurisdictions must develop watershed ... ...

    Abstract Regulatory watershed mitigation programs typically emphasize widespread adoption of best management practices (BMPs) to meet total maximum daily load (TMDL) goals. To comply with the Chesapeake Bay TMDL, jurisdictions must develop watershed implementation plans (WIPs) to determine the number and type of BMPs to implement. However, the spatial resolution of the bay-level model used to determine these load reduction goals is so coarse that the regulatory plan cannot consider heterogeneity in local conditions, which affects BMP effectiveness. Using the Topo-SWAT modification of the Soil and Water Assessment Tool (SWAT), we simulated two BMP adoption scenarios in the Spring Creek watershed in central Pennsylvania to determine if leveraging fine-scale spatial heterogeneity to place BMPs could achieve the same (or better) nutrient and sediment reduction at a lower cost than the state-level WIP BMP adoption recommendations. Topo-SWAT was initialized with detailed land use and management practice information, systematically calibrated, and validated against 12 yr of observed data. After determining individual BMP cost effectiveness, results were ranked to design a cost-effective BMP adoption scenario that achieved equal or greater load reduction as the WIP scenario for 74% of the cost using eight management-based BMPs: no-till, manure injection, cover cropping, riparian buffers, land retirement, manure application timing, wetland restoration, and nitrogen management (15% less N input). Because watersheds of this size typically represent the smallest modeling unit in the Chesapeake Bay Model, results demonstrate the potential to use watershed models with finer inference scales to improve recommendations for BMP implementation under the Chesapeake Bay TMDL.
    MeSH term(s) Conservation of Natural Resources ; Nitrogen/analysis ; Pennsylvania ; Soil ; Wetlands
    Chemical Substances Soil ; Nitrogen (N762921K75)
    Language English
    Publishing date 2020-03-25
    Publishing country United States
    Document type Journal Article
    ZDB-ID 120525-0
    ISSN 1537-2537 ; 0047-2425
    ISSN (online) 1537-2537
    ISSN 0047-2425
    DOI 10.1002/jeq2.20051
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  3. Article: Nutrient pollution

    Shortle, James S / Horan, Richard D

    Water economics and policy Vol. 3, No. 2 , p. 1-39

    a wicked challenge for economic instruments

    2017  Volume 3, Issue 2, Page(s) 1–39

    Author's details James Shortle and Richard D. Horan
    Keywords Multiple interacting pollutants ; spatial externalities ; stock externalities ; lagged discharges ; lagged ecosystem responses ; stochastic pollution ; deep uncertainty ; socio ; economic-ecological lands ; capes ; unintended consequences
    Language English
    Publisher World Scientific
    Publishing place Singapore
    Document type Article
    ZDB-ID 2920590-6
    Database ECONomics Information System

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  4. Article: Physical and enzymatic studies on poly d(I-C)-poly d(I-C), an unusual double-helical DNA.

    Mitsui, Y / Langridge, R / Shortle, B E / Cantor, C R / Grant, R C / Kodama, M / Wells, R D

    Nature

    1970  Volume 228, Issue 5277, Page(s) 1166–1169

    MeSH term(s) Circular Dichroism ; DNA/analysis ; DNA Nucleotidyltransferases ; Deoxyribonucleases ; Hydrogen-Ion Concentration ; Ligases ; Models, Structural ; Nucleic Acid Denaturation ; Phosphoric Monoester Hydrolases ; Phosphotransferases ; Polynucleotides/analysis ; RNA Nucleotidyltransferases ; X-Ray Diffraction
    Chemical Substances Polynucleotides ; DNA (9007-49-2) ; Phosphotransferases (EC 2.7.-) ; DNA Nucleotidyltransferases (EC 2.7.7.-) ; RNA Nucleotidyltransferases (EC 2.7.7.-) ; Deoxyribonucleases (EC 3.1.-) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2) ; Ligases (EC 6.-)
    Language English
    Publishing date 1970-12-19
    Publishing country England
    Document type Journal Article
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/2281166a0
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    Zs.A 26: Show issues Location:
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  5. Article: One sequence plus one mutation equals two folds

    Shortle, David

    Proceedings of the National Academy of Sciences of the United States of America. 2009 Dec. 15, v. 106, no. 50

    2009  

    Language English
    Dates of publication 2009-1215
    Size p. 21011-21012.
    Publishing place National Academy of Sciences
    Document type Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    Database NAL-Catalogue (AGRICOLA)

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  6. Article: Policy instruments for water quality protection

    Shortle, James / Horan, Richard D

    Annual review of resource economics Vol. 5 , p. 111-138

    2013  Volume 5, Page(s) 111–138

    Author's details James Shortle and Richard D. Horan
    Keywords Gewässerschutz ; Umweltökonomik ; Theorie
    Language English
    Publisher Annual Reviews
    Publishing place Palo Alto, Calif.
    Document type Article
    ZDB-ID 2527682-7
    ISSN 1941-1340
    Database ECONomics Information System

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  7. Article: Propensities, probabilities, and the Boltzmann hypothesis.

    Shortle, David

    Protein science : a publication of the Protein Society

    2003  Volume 12, Issue 6, Page(s) 1298–1302

    Abstract: The relative strengths of interactions involving polypeptide chains can be estimated with reasonable accuracy with statistical potentials, free-energy functions derived from the frequency of occurrence of structural arrangements of residues or atoms in ... ...

    Abstract The relative strengths of interactions involving polypeptide chains can be estimated with reasonable accuracy with statistical potentials, free-energy functions derived from the frequency of occurrence of structural arrangements of residues or atoms in collections of protein structures. Recent published work has shown that the energetics of side-chain/backbone interactions can be modeled by the phi/psi propensities of the 20 amino acids. In this report, the more commonly used phi/psi probabilities are demonstrated to fail in evaluating the free energies of protein conformations because of an overriding preference for all helical structures. Comparison of the hypothetical reactions implied by these two different statistics-propensities versus probabilities-leads to the conclusion that the Boltzmann hypothesis may only be applicable for the calculation of statistical potentials after the starting conformation has been specified. This conclusion supports a simple conjecture: The surprising success of the Boltzmann hypothesis in explaining the energetics of protein structures is a direct consequence of a real equilibrium, one extending over evolutionary time that has maintained the stability of each protein within a narrow range of values.
    MeSH term(s) Amino Acid Sequence ; Data Interpretation, Statistical ; Hydrogen Bonding ; Peptides/chemistry ; Probability ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins/chemistry ; Thermodynamics
    Chemical Substances Peptides ; Proteins
    Language English
    Publishing date 2003-06
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1110/ps.0306903
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Prediction of protein structure.

    Shortle, D

    Current biology : CB

    2000  Volume 10, Issue 2, Page(s) R49–51

    MeSH term(s) Protein Conformation ; Protein Folding
    Language English
    Publishing date 2000-01-27
    Publishing country England
    Document type Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/s0960-9822(00)00290-6
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    Zs.A 3208: Show issues Location:
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  9. Article: The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space.

    Shortle, David

    Advances in protein chemistry

    2002  Volume 62, Page(s) 1–23

    MeSH term(s) Magnetic Resonance Spectroscopy ; Models, Molecular ; Protein Conformation ; Protein Denaturation ; Proteins/chemistry
    Chemical Substances Proteins
    Language English
    Publishing date 2002-11-01
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 178-8
    ISSN 0065-3233
    ISSN 0065-3233
    DOI 10.1016/s0065-3233(02)62003-0
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  10. Article: Protein folding as seen from water's perspective.

    Shortle, D

    Nature structural biology

    1999  Volume 6, Issue 3, Page(s) 203–205

    MeSH term(s) Magnetic Resonance Spectroscopy ; Protein Conformation ; Protein Folding ; Scattering, Radiation ; Water/chemistry
    Chemical Substances Water (059QF0KO0R)
    Language English
    Publishing date 1999-03
    Publishing country United States
    Document type News
    ZDB-ID 1192623-5
    ISSN 1072-8368
    ISSN 1072-8368
    DOI 10.1038/6640
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