15491122

Source:http://linkedlifedata.com/resource/pubmed/id/15491122

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0033684, umls-concept:C0205245, umls-concept:C1707689
pubmed:issue	10
pubmed:dateCreated	2004-10-19
pubmed:abstractText	Metal-assembled parallel helix-bundle proteins have been used to investigate electron transfer through alpha-helical structures. Fermi Golden Rule distance dependence of electron transfer rates was established in a family of designed metalloproteins, and the contribution of intrahelical hydrogen bonding to the matrix tunneling element was explored. The first steps toward the design of functional proteins using dynamic combinatorial assembly of alpha-helical structural elements are described.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0157313
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Metalloproteins
pubmed:status	MEDLINE
pubmed:month	Oct
pubmed:issn	0001-4842
pubmed:author	pubmed-author:CaseMartin AMA, pubmed-author:McLendonGeorge LGL
pubmed:issnType	Print
pubmed:volume	37
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	754-62
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:15491122-Amino Acid Sequence, pubmed-meshheading:15491122-Metalloproteins, pubmed-meshheading:15491122-Molecular Sequence Data, pubmed-meshheading:15491122-Protein Conformation, pubmed-meshheading:15491122-Structure-Activity Relationship
pubmed:year	2004
pubmed:articleTitle	Metal-assembled modular proteins: toward functional protein design.
pubmed:affiliation	Department of Chemistry, The University of Vermont, Burlington, Vermont 05405, USA. martin.case@uvm.edu
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, Non-P.H.S.