The leucine binding proteins of Escherichia coli as models for studying the relationships between protein structure and function
dc.contributor.author | Antonucci, Tammy K. | en_US |
dc.contributor.author | Landick, Robert C. | en_US |
dc.contributor.author | Oxender, Dale L. | en_US |
dc.date.accessioned | 2006-04-28T16:58:41Z | |
dc.date.available | 2006-04-28T16:58:41Z | |
dc.date.issued | 1985 | en_US |
dc.identifier.citation | Antonucci, Tammy K.; Landick, Robert; Oxender, Dale L. (1985)."The leucine binding proteins of Escherichia coli as models for studying the relationships between protein structure and function." Journal of Cellular Biochemistry 29(3): 209-216. <http://hdl.handle.net/2027.42/38447> | en_US |
dc.identifier.issn | 0730-2312 | en_US |
dc.identifier.issn | 1097-4644 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/38447 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4077929&dopt=citation | en_US |
dc.description.abstract | The genes encoding the leucine binding proteins in E coli have been cloned and their DNA sequences have been determined. One of the binding proteins (LIV-BP) binds leucine, isoleucine, valine, threonine, and alanine, whereas the oilier (LS-BP) binds only the D- and L-isomers of leucine. These proteins bind their solutes as they enter the periplasm, then interact with three membrane components, livH, livG, and livM, to achieve the translocation of the solute across the bacterial cell membrane. Another feature of the binding proteins is that they must be secreted into the periplasmic space where they carry out their function. The amino acid sequence of the two binding proteins is 80% homologous, indicating that they arc the products of an ancestral gene duplication. Because of these characteristics of the leucine binding proteins, we are using them as models for studying the relationships between protein structure and function. | en_US |
dc.format.extent | 427464 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Wiley Subscription Services, Inc., A Wiley Company | en_US |
dc.subject.other | Life and Medical Sciences | en_US |
dc.subject.other | Cell & Developmental Biology | en_US |
dc.title | The leucine binding proteins of Escherichia coli as models for studying the relationships between protein structure and function | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Genetics | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109 | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109 | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109 | en_US |
dc.identifier.pmid | 4077929 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/38447/1/240290305_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/jcb.240290305 | en_US |
dc.identifier.source | Journal of Cellular Biochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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