Please note, due to essential maintenance online transactions will not be possible between 02:30 and 04:00 BST, on Tuesday 17th September 2019 (22:30-00:00 EDT, 17 Sep, 2019). We apologise for any inconvenience.
To send content items to your account,
please confirm that you agree to abide by our usage policies.
If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account.
Find out more about sending content to .
To send content items to your Kindle, first ensure firstname.lastname@example.org
is added to your Approved Personal Document E-mail List under your Personal Document Settings
on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part
of your Kindle email address below.
Find out more about sending to your Kindle.
Note you can select to send to either the @free.kindle.com or @kindle.com variations.
‘@free.kindle.com’ emails are free but can only be sent to your device when it is connected to wi-fi.
‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.
The crystal structure of ribosomal protein L5 from Thermus
thermophilus complexed with a 34-nt fragment comprising
helix III and loop C of Escherichia coli 5S rRNA has
been determined at 2.5 Å resolution. The protein specifically
interacts with the bulged nucleotides at the top of loop C of
5S rRNA. The rRNA and protein contact surfaces are strongly
stabilized by intramolecular interactions. Charged and polar
atoms forming the network of conserved intermolecular hydrogen
bonds are located in two narrow planar parallel layers belonging
to the protein and rRNA, respectively. The regions, including
these atoms conserved in Bacteria and Archaea, can be considered
an RNA–protein recognition module. Comparison of the T.
thermophilus L5 structure in the RNA-bound form with the
isolated Bacillus stearothermophilus L5 structure shows
that the RNA-recognition module on the protein surface does
not undergo significant changes upon RNA binding. In the crystal
of the complex, the protein interacts with another RNA molecule
in the asymmetric unit through the β-sheet concave surface.
This protein/RNA interface simulates the interaction of L5 with
23S rRNA observed in the Haloarcula marismortui 50S
Bovine αs1-casein F (αs1-CN F)
was found in a genetic resource of
Deutsches Schwarzbuntes Niederungsrind cows at a frequency of 0·009.
characterization of this new variant was obtained by automated sequencing
reversed-phase HPLC-separated tryptic peptides of αs1-CN
and αs1-CN B. αs1-CN F was found to be
subtype of αs1-CN B with a single amino acid substitution
(SerP/Leu) in position 66. DNA sequencing revealed a C/T transition
8418 of the gene. Sequence-specific primers were designed to perform an
polymerase chain reaction for detection of αs1CnF.
Typing of artificial insemination sperm samples included in the genetic
sperm pool identified one sire heterozygous for αs1CnF.
Email your librarian or administrator to recommend adding this to your organisation's collection.