1 Ocak 1994 Dergi makalesi Açık Erişim

JERNIGAN, R; RAGHUNATHAN, G; BAHAR, I

DataCite XML

<?xml version='1.0' encoding='utf-8'?>
<resource xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns="http://datacite.org/schema/kernel-4" xsi:schemaLocation="http://datacite.org/schema/kernel-4 http://schema.datacite.org/meta/kernel-4.1/metadata.xsd">
  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/103983</identifier>
  <creators>
    <creator>
      <creatorName>JERNIGAN, R</creatorName>
      <givenName>R</givenName>
      <familyName>JERNIGAN</familyName>
    </creator>
    <creator>
      <creatorName>RAGHUNATHAN, G</creatorName>
      <givenName>G</givenName>
      <familyName>RAGHUNATHAN</familyName>
    </creator>
    <creator>
      <creatorName>BAHAR, I</creatorName>
      <givenName>I</givenName>
      <familyName>BAHAR</familyName>
    </creator>
  </creators>
  <titles>
    <title>Characterization Of Interactions And Metal-Ion Binding-Sites In Proteins</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>1994</publicationYear>
  <dates>
    <date dateType="Issued">1994-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/103983</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsVersionOf">10.81043/aperta.103982</relatedIdentifier>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.81043/aperta.103983</relatedIdentifier>
  </relatedIdentifiers>
  <rightsList>
    <rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
  </rightsList>
  <descriptions>
    <description descriptionType="Abstract">Recent investigations show that as a class of interactions for designing proteins, hydrophobic interactions are not specific enough, hydrophilic interactions are typically too weak, and water interactions are always on the exterior. In terms of overall protein stability, there is a substantial advantage to a nucleus with strong, directional interactions. Metal ion sites in proteins exhibit strong directional preferences for their coordinate ligands, and the specificities manifested by ions have been demonstrated to be useful in reducing molecular fluctuations. The engineered introduction of zinc binding sites has been shown to improve the stabilities of designed proteins. Metal binding sites can therefore provide important structural building blocks for protein design.</description>
  </descriptions>
</resource>