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      Structure and dynamics of the neutrophil defensins NP-2, NP-5, and HNP-1: NMR studies of amide hydrogen exchange kinetics.

      1 , ,
      Proteins
      Wiley

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          Abstract

          The exchange kinetics for the slowly exchanging amide hydrogens in three defensins, rabbit NP-2, rabbit NP-5, and human HNP-1, have been measured over a range of pH at 25 degrees C using 1D and 2D NMR methods. These NHs have exchange rates 10(2) to 10(5) times slower than rates from unstructured model peptides. The observed distribution of exchange rates under these conditions can be rationalized by intramolecular hydrogen bonding of the individual NHs, solvent accessibility of the NHs, and local fluctuations in structure. The temperature dependencies of NH chemical shifts (NH temperature coefficients) were measured for the defensins and these values are consistent with the defensin structure. A comparison is made between NH exchange kinetics, NH solvent accessibility, and NH temperature coefficients of the defensins and other globular proteins. Titration of the histidine side chain in NP-2 was examined and the results are mapped to the three-dimensional structure.

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          Author and article information

          Journal
          Proteins
          Proteins
          Wiley
          0887-3585
          0887-3585
          Sep 1994
          : 20
          : 1
          Affiliations
          [1 ] Department of Chemistry and Biochemistry, University of Colorado-Boulder 80309-0215.
          Article
          10.1002/prot.340200107
          7824523
          87221dcf-fc6a-43a6-bbf8-439c2122a345
          History

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