<div class="sw-email-modal sw--display-block"> <div id="emailModalContentContainer"> <span class="noty_close sw--position-absolute sw--position-right sw--padding-top-3 sw--padding-right-3 icon-cancel sw--opacity-8"></span> <div class="sw-row"> <div class="sw-email-modal__copy sw--position-relative sw--display-block sw--padding-vert-4"> <p class="last sw--font-size-16">Sign up to get email alerts on discount promotions. There might be one very soon...</p> <form action="/register/email-signup" class="sw-email-modal__signup sw--position-relative" data-confirmation="emailConfirmationModal" data-sw-email-modal-form> <input type="text" class="sw-email-modal__signup-input sw--input-height__medium" placeholder="Email address" name="email" /> <input type="hidden" class="sw-email-modal__signup-input" name="location" value="/product/3CBNJ5CY9/ribose-binding-protein-ribbon-2dri" /> <input type="hidden" class="sw-email-modal__signup-input" name="confirmation" value="emailConfirmationModal" /> <input type="submit" class="btn-primary" value="Sign Up" /> <div id="emailModalFormError" class="text-error" style="display:none"></div> </form> </div> </div> </div>

Click and drag to rotate
Ribose Binding Protein Ribbon (2DRI) 3d printed

DIGITAL PREVIEW
Not a Photo

Coated Full Color Sandstone
Ribose Binding Protein Ribbon (2DRI) 3d printed
Ribose Binding Protein Ribbon (2DRI) 3d printed

DIGITAL PREVIEW
Not a Photo

Ribose Binding Protein Ribbon (2DRI)

Made By
Size
OVERVIEW
  • 3D printed in Coated Full Color Sandstone: Fully colored material with a glossy and smooth finish.
  • Be the first to try. Learn more
  • This product is intended for mature audiences.
$96.97
1
0
Share Link
Embed This Product

Product Description

A number of mutations at Gly134 of the periplasmic ribose-binding protein of Escherichia coli were examined by a combined biochemical and structural approach. Different mutations gave rise to different patterns of effects on the chemotaxis and transport functions. The smallest residue (alanine) had the least effect on transport, whereas large hydrophobic residues had the smallest effect on chemotaxis. Comparison of the x-ray crystal structure of the G134R mutant protein (2.5-A resolution) to that of the wild type (1.6-A resolution) showed that the basic structure of the protein was unaltered. The loss of chemotaxis and transport functions in this and similar mutant proteins must therefore be caused by relatively simple surface effects, which include a change in local main chain conformation. The loss of chemotaxis and transport functions resulting from the introduction of an alanine residue at position 134 was suppressed by an additional isoleucine to threonine mutation at residue 132. An x-ray structure of the I132T/G134A double mutant protein (2.2-A resolution) showed that the changes in local structure were accompanied by a diffuse pattern of structural changes in the surrounding region, implying that the suppression derives from a combination of sources. 
http://www.rcsb.org/pdb/explore.do?structureId=2DRI
What's in the Box
INCM
RiboseBindingProtein Max 1
Coated Full Color Sandstone
Width
5.9 cm
Height
10.2 cm
Depth
6.4 cm

Sign In or Join to comment.
 
 
Logo

Hello.

We're sorry to inform you that we no longer support this browser and can't confirm that everything will work as expected. For the best Shapeways experience, please use one of the following browsers:

Click anywhere outside this window to continue.