Search: id:"swepub:oai:lup.lub.lu.se:2d4971fe-c16a-4898-b4cd-f13cfc0c36a4" >
Investigation at Re...
Investigation at Residue Level of the Early Steps during the Assembly of Two Proteins into Supramolecular Objects
-
Salvatore, Delphine B. (author)
-
Duraffourg, Nicolas (author)
-
Favier, Adrien (author)
-
show more...
-
- Persson, Björn (author)
- Lund University,Lunds universitet,Beräkningskemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Computational Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
-
- Lund, Mikael (author)
- Lund University,Lunds universitet,Beräkningskemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Computational Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
-
Delage, Marie-Madeleine (author)
-
Silvers, Robert (author)
-
Schwalbe, Harald (author)
-
Croguennec, Thomas (author)
-
Bouhallab, Said (author)
-
Forge, Vincent (author)
-
show less...
-
(creator_code:org_t)
- 2011-05-13
- 2011
- English.
-
In: Biomacromolecules. - : American Chemical Society (ACS). - 1526-4602 .- 1525-7797. ; 12:6, s. 2200-2210
- Related links:
-
http://dx.doi.org/10...
-
show more...
-
https://lup.lub.lu.s...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- Understanding the driving forces governing protein assembly requires the characterization of interactions at molecular level. We focus on two homologous oppositely charged proteins, lysozyme and alpha-lactalbumin, which can assemble into microspheres. The assembly early steps were characterized through the identification of interacting surfaces monitored at residue level by NMR chemical shift perturbations by titrating one N-15-labeled protein with its unlabeled partner. While a-lactalbumin has a narrow interacting site, lysozyme has interacting sites scattered on a broad surface. The further assembly of these rather unspecific heterodimers into tetrarners leads to the establishment of well-defined interaction sites. Within the tetramers, most of the electrostatic charge patches on the protein surfaces are shielded. Then, hydrophobic interactions, which are possible because alpha-lactalbumin is in a partially folded state, become preponderant, leading to the formation of larger oligomers. This approach will be particularly useful for rationalizing the design of protein assemblies as nanoscale devices.
Subject headings
- NATURVETENSKAP -- Kemi -- Teoretisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Theoretical Chemistry (hsv//eng)
Publication and Content Type
- art (subject category)
- ref (subject category)
Find in a library
To the university's database
- By the author/editor
-
Salvatore, Delph ...
-
Duraffourg, Nico ...
-
Favier, Adrien
-
Persson, Björn
-
Lund, Mikael
-
Delage, Marie-Ma ...
-
show more...
-
Silvers, Robert
-
Schwalbe, Harald
-
Croguennec, Thom ...
-
Bouhallab, Said
-
Forge, Vincent
-
show less...
- About the subject
-
- NATURAL SCIENCES
-
NATURAL SCIENCES
-
and Chemical Science ...
-
and Theoretical Chem ...
- Articles in the publication
-
Biomacromolecule ...
- By the university
-
Lund University