Detalhe da pesquisa
1.
Conformational analysis of a mitochondrial presequence derived from the F1-ATPase beta-subunit by CD and NMR spectroscopy.
Biochim Biophys Acta
; 1159(1): 81-93, 1992 Sep 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-1390913
2.
Two-dimensional J-resolved proton NMR spectroscopy of oligomannosidic glycopeptides.
J Biol Chem
; 257(7): 3409-13, 1982 Apr 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-7061488
3.
Comparison of helix stability in wild-type and mutant LamB signal sequences.
J Biol Chem
; 265(7): 3851-8, 1990 Mar 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-2406265
4.
Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an alpha-helical region of carboxypeptidase A.
Proteins
; 10(2): 130-9, 1991.
Artigo
em Inglês
| MEDLINE | ID: mdl-1896426
5.
Impact of a micellar environment on the conformations of two cyclic pentapeptides.
Biopolymers
; 32(12): 1741-54, 1992 Dec.
Artigo
em Inglês
| MEDLINE | ID: mdl-1472656
6.
Helix formation and stability in a signal sequence.
Biochemistry
; 28(21): 8554-61, 1989 Oct 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-2605206
7.
Design and characterization of a model alpha beta peptide.
Biopolymers
; 36(2): 109-20, 1995 Aug.
Artigo
em Inglês
| MEDLINE | ID: mdl-7492740
8.
Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments.
Biochemistry
; 32(18): 4881-94, 1993 May 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-8387821
9.
Cyclic pentapeptides as models for reverse turns: determination of the equilibrium distribution between type I and type II conformations of Pro-Asn and Pro-Ala beta-turns.
Biopolymers
; 29(1): 263-87, 1990 Jan.
Artigo
em Inglês
| MEDLINE | ID: mdl-2328290
10.
Characterization of virtual coupling in the proton nuclear magnetic resonance spectrum of N,N'-diacetylchitobiose by two-dimensional J-resolved spectroscopy.
Biochem Biophys Res Commun
; 123(2): 555-61, 1984 Sep 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-6487300