Related ArticlesAn NMR study on the beta-hairpin region of barnase.
Fold Des. 1996;1(3):231-41
Authors: Neira JL, Fersht AR
BACKGROUND: The beta-hairpin of barnase (residues Ser92-Leu95) has been proposed in theoretical and protein engineering studies to be an initiation site for folding [1]. There is evidence for residual structure in this region from NMR studies of the denatured protein under different denaturing conditions [2,3]. A more detailed analysis is possible by NMR studies of isolated fragments. RESULTS: Protons of fragments B(80-110) and B(69-110) in 6 M urea have non-random chemical shifts. Non-native long-range and medium-range NOE contacts with the aromatic moiety of Trp94 indicate that it is involved in a beta-turn-like or alpha-helix-like conformation. Also, the sidechains of Trp71, Tyr79, Phe82, Tyr90, Tyr97, His102, Tyr103 and Phe106 show non-native hydrophobic contacts. Non-random conformational shifts and sequential NN(i,i+1) NOE contacts are clustered to one of the beta-strands and one of the loop regions. CONCLUSIONS: The hairpin region of barnase adopts beta-turn-like or alpha-helix-like conformations, which are weakly populated even in 6 M urea. The hairpin region is a potential nucleation site in folding that may consolidate on docking with the first alpha-helix. The other residues that have conformational preferences from a beta-strand and one of the loop regions in the native intact protein, but they do not constitute a nucleation site.
[NMR paper] Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxatio
Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxation.
Related Articles Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxation.
Protein Sci. 1998 Mar;7(3):720-9
Authors: Ramirez-Alvarado M, Daragan VA, Serrano L, Mayo KH
Structurally characterizing partially folded peptides is problematic given the nature of their transient conformational states. 13C-NMR relaxation data can provide information on the geometry of bond rotations, motional restrictions, and correlated bond rotations...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
[NMR paper] Native-like beta-hairpin structure in an isolated fragment from ferredoxin: NMR and C
Native-like beta-hairpin structure in an isolated fragment from ferredoxin: NMR and CD studies of solvent effects on the N-terminal 20 residues.
Related Articles Native-like beta-hairpin structure in an isolated fragment from ferredoxin: NMR and CD studies of solvent effects on the N-terminal 20 residues.
Protein Eng. 1996 Jul;9(7):559-65
Authors: Searle MS, Zerella R, Williams DH, Packman LC
The conformational properties of protein fragments have been widely studied as models of the earliest initiation events in protein folding. While...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] High helicity of peptide fragments corresponding to beta-strand regions of beta-lacto
High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
Related Articles High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
Fold Des. 1996;1(4):255-63
Authors: Kuroda Y, Hamada D, Tanaka T, Goto Y
BACKGROUND: Whereas protein fragments, when they are structured, adopt conformations similar to that found in the native state, the high helical propensity of beta-lactoglobulin, a predominantly beta-sheet...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment compleme
NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment complementation.
Related Articles NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment complementation.
Proteins. 1995 May;22(1):41-4
Authors: Tasayco ML, Chao K
The study of complementary protein fragments is thought to be generally useful to identify early folding intermediates. A prerequisite for these studies is the reconstitution of the native-like structure by fragment complementation. Structural analysis of the complementation of the...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensio
High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Related Articles High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Science. 1994 Mar 25;263(5154):1762-7
Authors: Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM
The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensio
High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Related Articles High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Science. 1994 Mar 25;263(5154):1762-7
Authors: Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM
The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] An NMR study of the HIV-1 TAR element hairpin.
An NMR study of the HIV-1 TAR element hairpin.
Related Articles An NMR study of the HIV-1 TAR element hairpin.
Biochemistry. 1993 Nov 23;32(46):12522-30
Authors: Jaeger JA, Tinoco I
The TAR hairpin is an important part of the 5' long terminal repeat of HIV-1 and appears to be recognized by a cellular protein. A 14-base model of the native TAR hairpin 5'-GAGC-GCUC-3' (loop bases in square brackets) has been studied by proton, phosphorus, and natural abundance carbon NMR; these results are compared to other published NMR studies of the TAR...
nmrlearner
Journal club
0
08-22-2010 03:01 AM
[NMR paper] A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escheric
A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli.
Protein Sci. 1993 Nov;2(11):1938-47
Authors: Sun ZY, Truong HT, Pratt EA, Sutherland DC,...
An NMR study on the beta-hairpin region of barnase.
Linear Mode
