Articles citing this article

The Citing articles tool gives a list of articles citing the current article.
The citing articles come from EDP Sciences database, as well as other publishers participating in CrossRef Cited-by Linking Program. You can set up your personal account to receive an email alert each time this article is cited by a new article (see the menu on the right-hand side of the abstract page).

Cited article:

NMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteins

Tai‐He Xia, John H. Bushweller, Patrick Sodano, Martin Billeter, Olof Björnberg, Arne Holmgren and Kurt Wüthrich
Protein Science 1 (3) 310 (1992)
https://doi.org/10.1002/pro.5560010302

Proton, carbon-13, and nitrogen-15 NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteins

Michael Wittekind, Matthias Gorlach, Mark Friedrichs, Gideon Dreyfuss and Luciano Mueller
Biochemistry 31 (27) 6254 (1992)
https://doi.org/10.1021/bi00142a013

Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation

Carol A. Rohl, J. Martin Scholtz, Eunice J. York, John M. Stewart and Robert L. Baldwin
Biochemistry 31 (5) 1263 (1992)
https://doi.org/10.1021/bi00120a001

Proton NMR studies of Cucurbita maxima trypsin inhibitors: evidence for pH-dependent conformational change and His25-Tyr27 interaction

Ramaswamy Krishnamoorthi, Chan Lan Sun Lin, Yu Xi Gong, David VanderVelde and Karl Hahn
Biochemistry 31 (3) 905 (1992)
https://doi.org/10.1021/bi00118a037

Peptide secondary structure induced by a micellar phospholipidic interface: proton NMR conformational study of a lipopeptide

Francois Macquaire, Francoise Baleux, Emmanuelle Giaccobi, Huynh Dinh Tam, Jean Michel Neumann and Alain Sanson
Biochemistry 31 (9) 2576 (1992)
https://doi.org/10.1021/bi00124a018

Proton NMR assignments and secondary structure of human .beta.2-microglobulin in solution

Mark Okon, Paul Bray and Dusan Vucelic
Biochemistry 31 (37) 8906 (1992)
https://doi.org/10.1021/bi00152a030

The two polypeptide chains in fibronectin are joined in antiparallel fashion: NMR structural characterization

Seong Soo A. An, Jesus Jimenez-Barbero, Torben E. Petersen and Miguel Llinas
Biochemistry 31 (41) 9927 (1992)
https://doi.org/10.1021/bi00156a010

Comparison of conformational features of staphylococcal nuclease in ternary complexes with pdTp, pdGp, and nitrophenyl-pdTp

Susan M. Stanczyk and Philip H. Bolton
Biochemistry 31 (28) 6396 (1992)
https://doi.org/10.1021/bi00143a006

NMR study of parallel-stranded tetraplex formation by the hexadeoxynucleotide d(TG4T)

Fareed Aboul-ela, Alastair I. H. Murchie and David M. J. Lilley
Nature 360 (6401) 280 (1992)
https://doi.org/10.1038/360280a0

Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals

Martin Billeter
Quarterly Reviews of Biophysics 25 (3) 325 (1992)
https://doi.org/10.1017/S0033583500004261

Nonlocal structural perturbations in a mutant human insulin: sequential resonance assignment and carbon-13-labeled-isotope-aided 2D-NMR studies of [PheB24.fwdarw.Gly]insulin with implications for receptor recognition

Qing Xin Hua, Steven E. Shoelson and Michael A. Weiss
Biochemistry 31 (47) 11940 (1992)
https://doi.org/10.1021/bi00162a037

Sequential resonance assignments of oxidized high-potential iron-sulfur protein from Chromatium vinosum

David G. Nettesheim, Scott R. Harder, Benjamin A. Feinberg and James D. Otvos
Biochemistry 31 (4) 1234 (1992)
https://doi.org/10.1021/bi00119a037

Three-dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution

Milton H. Werner and David E. Wemmer
Biochemistry 31 (4) 999 (1992)
https://doi.org/10.1021/bi00119a008

Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions

Daisuke Kohda and Fuyuhiko Inagaki
Biochemistry 31 (47) 11928 (1992)
https://doi.org/10.1021/bi00162a036

1H‐NMR conformational study of a synthetic peptide derived from the consensus sequence of Annexins

FRANÇOIS MACQUAIRE, FRANÇOISE BALEUX, TAM HUYNH‐DINH, JEAN MICHEL NEUMANN and ALAIN SANSON
International Journal of Peptide and Protein Research 39 (2) 117 (1992)
https://doi.org/10.1111/j.1399-3011.1992.tb00780.x

Linear and cyclic peptide analogues of the polypeptide cardiac stimulant, anthopleurin‐A

Alison R. GOULD, Bridget C. MABBUTT, Lyndon E. LLEWELLYN, Neil H. GOSS and Raymond S. NORTON
European Journal of Biochemistry 206 (3) 641 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb16969.x

Sequence-specific assignments of the proton nuclear magnetic resonance spectra of reduced high-potential ferredoxin (HiPIP) from Chromatium vinosum

Jacques Gaillard, Jean Pierre Albrand, Jean Marc Moulis and David E. Wemmer
Biochemistry 31 (24) 5632 (1992)
https://doi.org/10.1021/bi00139a029

Nucleic acid interactive properties of a peptide corresponding to the N-terminal zinc finger domain of HIV-1 nucleocapsid protein

Martha D. Delahunty, Terri L. South, Michael F. Summers and Richard L. Karpel
Biochemistry 31 (28) 6461 (1992)
https://doi.org/10.1021/bi00143a015

Determination of the secondary structure and folding topology of human interleukin-4 using three-dimensional heteronuclear magnetic resonance spectroscopy

Daniel S. Garrett, Robert Powers, Carl J. March, Eric A. Frieden, G. Marius Clore and Angela M. Gronenborn
Biochemistry 31 (17) 4347 (1992)
https://doi.org/10.1021/bi00132a027

A .beta.-turn is present in the 392-411 segment of the human fibrinogen .gamma.-chain. Effects of structural changes in this segment on affinity to antibody 4A5

Michael Blumenstein, Gary R. Matsueda, Sheila Timmons and Jacek Hawiger
Biochemistry 31 (44) 10692 (1992)
https://doi.org/10.1021/bi00159a008

Solution conformation of a peptide corresponding to the principal neutralizing determinant of HIV-1IIIB: a two-dimensional NMR study

Anat Zvi, Reuben Hiller and Jacob Anglister
Biochemistry 31 (30) 6972 (1992)
https://doi.org/10.1021/bi00145a015

Sequence‐specific 1H‐NMR assignment and determination of the secondary structure of bovine heart fatty‐acid‐binding protein

Christian LÜCKE, Dirck LASSEN, Hans‐Jürgen KREIENKAMP, Friedrich SPENER and Heinz RÜTERJANS
European Journal of Biochemistry 210 (3) 901 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17494.x

Three-dimensional homonuclear NOESY-TOCSY of an intramolecular pyrimidine.cntdot.purine.cntdot.pyrimidine DNA triplex containing a central G.cntdot.TA triple: nonexchangeable proton assignments and structural implications

Ishwar Radhakrishnan, Dinshaw J. Patel and Xiaolian Gao
Biochemistry 31 (9) 2514 (1992)
https://doi.org/10.1021/bi00124a011

Determination of the three‐dimensional solution structure of the histidine‐containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy

Nico A. J. van NULAND, Joachim GRÖTZINGER, Klaas DIJKSTRA, Ruud M. SCHEEK and George T. ROBILLARD
European Journal of Biochemistry 210 (3) 881 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17492.x

Solution conformation of a cyclic pentapeptide endothelin antagonist Comparison of structures obtained from constrained dynamics and conformational search

Stanley R. Krystek, Donna A. Bassolino, Robert E. Bruccoleri, John T. Hunt, Michael A. Porubcan, Charles F. Wandler and Niels H. Andersen
FEBS Letters 299 (3) 255 (1992)
https://doi.org/10.1016/0014-5793(92)80127-3

NMR studies of amyloid .beta.-peptides: proton assignments, secondary structure, and mechanism of an .alpha.-helix .fwdarw. .beta.-sheet conversion for a homologous, 28-residue, N-terminal fragment

Michael G. Zagorski and Colin J. Barrow
Biochemistry 31 (24) 5621 (1992)
https://doi.org/10.1021/bi00139a028

Formate as an NMR probe of anion binding to copper-zinc and copper-cobalt bovine erythrocyte superoxide dismutase

Marco Sette, Maurizio Paci, Alessandro Desideri and Giuseppe Rotilio
Biochemistry 31 (49) 12410 (1992)
https://doi.org/10.1021/bi00164a016

Structural studies of Desulfovibrio vulgaris ferrocytochrome c3 by two‐dimensional NMR

David L. TURNER, Carlos A. SALGUEIRO, Jean LeGALL and António V. XAVIER
European Journal of Biochemistry 210 (3) 931 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17497.x

Solution structure of the fifth repeat of factor H: a second example of the complement control protein module

P. N. Barlow, D. G. Norman, A. Steinkasserer, T. J. Horne, J. Pearce, P. C. Driscoll, R. B. Sim and I. D. Campbell
Biochemistry 31 (14) 3626 (1992)
https://doi.org/10.1021/bi00129a011

Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding

Magnus Ullner, Maria Selander, Egon Persson, Johan Stenflo, Torbjoern Drakenberg and Olle Teleman
Biochemistry 31 (26) 5974 (1992)
https://doi.org/10.1021/bi00141a004

Sequential proton and nitrogen-15 NMR assignments and secondary structure of a recombinant anti-digoxin antibody VL domain

Keith L. Constantine, Valentina Goldfarb, Michael Wittekind, James Anthony, Shi Chung Ng and Luciano Mueller
Biochemistry 31 (21) 5033 (1992)
https://doi.org/10.1021/bi00136a017

Effects of the presence of an aldehydic abasic site on the thermal stability and rates of helix opening and closing of duplex DNA

Igor Goljer, Jane M. Withka, Jung Yie Kao and Philip H. Bolton
Biochemistry 31 (46) 11614 (1992)
https://doi.org/10.1021/bi00161a047

The secondary structure of the colicin E3 immunity protein as studied by proton-proton and proton-nitrogen-15 two-dimensional NMR spectroscopy

Shunsuke Yajima, Yutaka Muto, Shigeyuki Yokoyama, Haruhiko Masaki and Takeshi Uozumi
Biochemistry 31 (24) 5578 (1992)
https://doi.org/10.1021/bi00139a022

Secondary structure of human granulocyte colony‐stimulating factor derived from NMR spectroscopy

Thomas Zink, Alfred Ross, Dorothee Ambrosius, Rainer Rudolph and Tad A. Holak
FEBS Letters 314 (3) 435 (1992)
https://doi.org/10.1016/0014-5793(92)81521-M

A new constraint potential for the structure refinement of biomolecules in solution using experimental nuclear overhauser effect intensity

Bernard Stawarz, Monique Genest and Daniel Genest
Biopolymers 32 (6) 633 (1992)
https://doi.org/10.1002/bip.360320606

NMR and molecular modeling characterization of RGD containing peptides

M.J. BOGUSKY, A.M. NAYLOR, S.M. PITZENBERGER, R.F. NUTT, S.F. BRADY, C.D. COLTON, J.T. SISKO, P.S. ANDERSON and D.F. VEBER
International Journal of Peptide and Protein Research 39 (1) 63 (1992)
https://doi.org/10.1111/j.1399-3011.1992.tb01557.x

Solution structure of the covalent sterigmatocystin-DNA adduct

S. Gopalakrishnan, Xiucai Liu and Dinshaw J. Patel
Biochemistry 31 (44) 10790 (1992)
https://doi.org/10.1021/bi00159a021

Solution Conformation of Gramicidin S Determined by Nuclear Magnetic Resonance and Distance Geometry Calculation

Chin Yu, Jan‐Fu Hwang, Chao‐Jung Yeh and Li‐Chin Chuang
Journal of the Chinese Chemical Society 39 (3) 231 (1992)
https://doi.org/10.1002/jccs.199200039

Studies of DNA dumbbells. II. Construction and characterization of DNA dumbbells with a 16 base‐pair duplex stem and Tn end loops (n = 2, 3, 4, 6, 8, 10, 14)

Mohan Amaratunga, Elizabeth Snowden‐Ifft, David E. Wemmer and Albert S. Benight
Biopolymers 32 (7) 865 (1992)
https://doi.org/10.1002/bip.360320713

The three‐dimensional structure of the first EGF‐like module of human factor IX: Comparison with EGF and TGF‐α

M. Baron, D.G. Norman, T.S. Harvey, I.D. Campbell, P.A. Handford, M. Mayhew, G.G. Brownlee and A.G.D. Tse
Protein Science 1 (1) 81 (1992)
https://doi.org/10.1002/pro.5560010109

Spectroscopic study of the interaction between poly‐(9‐vinyladenine) and single or multistrand RNA

Eiji Yashima, Teruyo Tajima, Noriyuki Miyauchi and Mitsuru Akashi
Biopolymers 32 (7) 811 (1992)
https://doi.org/10.1002/bip.360320709

NMR study on solution structure of the site‐specific mutant Leu48→Ala transforming growth factor alpha§

TAMMY PAGE KLINE and LUCIANO MUELLER
International Journal of Peptide and Protein Research 39 (2) 111 (1992)
https://doi.org/10.1111/j.1399-3011.1992.tb00779.x

Proton NMR assignment and secondary structure of the cell adhesion type III module of fibronectin

Martin Baron, Alison L. Main, Paul C. Driscoll, Helen J. Mardon, Jonathan Boyd and Iain D. Campbell
Biochemistry 31 (7) 2068 (1992)
https://doi.org/10.1021/bi00122a025

Proton resonance assignments and three-dimensional solution structure of the ragweed allergen Amb a V by nuclear magnetic resonance spectroscopy

William J. Metzler, Kathleen Valentine, Marianne Roebber, David G. Marsh and Luciano Mueller
Biochemistry 31 (37) 8697 (1992)
https://doi.org/10.1021/bi00152a003

NMR restraint analysis of transforming growth factor α: A key component for NMR structure refinement

Frank K. Brown, Judith C. Hempel and Peter W. Jeffs
Proteins: Structure, Function, and Bioinformatics 13 (4) 306 (1992)
https://doi.org/10.1002/prot.340130404

Studies of protein hydration in aqueous solution by high‐resolution nuclear magnetic resonance spectroscopy

Kurt Wüthrich and Gottfried Otting
International Journal of Quantum Chemistry 42 (5) 1553 (1992)
https://doi.org/10.1002/qua.560420528

Secondary structure in solution of barwin from barley seed using proton nuclear magnetic resonance spectroscopy

Svend Ludvigsen and Flemming M. Poulsen
Biochemistry 31 (37) 8771 (1992)
https://doi.org/10.1021/bi00152a013

Phosphorus-31 NMR spectra of oligodeoxyribonucleotide duplex lac operator-repressor headpiece complexes: importance of phosphate ester backbone flexibility in protein-DNA recognition

Christine Karslake, Maria Victoria Botuyan and David G. Gorenstein
Biochemistry 31 (6) 1849 (1992)
https://doi.org/10.1021/bi00121a038

Solution structure of a synthetic peptide corresponding to a receptor binding region of FSH (hFSH-β 33–53)

Paul F. Agris, Richard H. Guenther, Hanna Sierzputowska-Gracz, Laura Easter, Wanda Smith, Charles C. Hardin, Tomás A. Santa-Coloma, John W. Crabb and Leo E. Reichert
Journal of Protein Chemistry 11 (5) 495 (1992)
https://doi.org/10.1007/BF01025027

The shapes of backbones of chain molecules: Three‐dimensional characterization by spherical shape maps

Gustavo A. Arteca and Paul G. Mezey
Biopolymers 32 (12) 1609 (1992)
https://doi.org/10.1002/bip.360321204

Solution structure of a trinucleotide A-T-A bulge loop within a DNA duplex

Mark A. Rosen, Lawrence Shapiro and Dinshaw J. Patel
Biochemistry 31 (16) 4015 (1992)
https://doi.org/10.1021/bi00131a017

Conformation/activity studies of rationally designed potent anti‐adhesive RGD peptides

Marion GURRATH, Gerhard MÜLLER, Horst KESSLER, Monique AUMAILLEY and Rupert TIMPL
European Journal of Biochemistry 210 (3) 911 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17495.x

Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments

Helen R. Mott, Paul C. Driscoll, Jonathan Boyd, Robert M. Cooke, Malcolm P. Weir and Iain D. Campbell
Biochemistry 31 (33) 7741 (1992)
https://doi.org/10.1021/bi00148a040

Molecular analysis of the protein‐protein interaction between the E9 immunity protein and colicin E9

Russell WALLIS, Geoffrey R. MOORE, Colin KLEANTHOUS and Richard JAMES
European Journal of Biochemistry 210 (3) 923 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17496.x

Comparative NMR study of An-bulge loops in DNA duplexes: intrahelical stacking of A, A-A, and A-A-A bulge loops

Mark A. Rosen, David Live and Dinshaw J. Patel
Biochemistry 31 (16) 4004 (1992)
https://doi.org/10.1021/bi00131a016

Conformation and dynamics of an Fab'-bound peptide by isotope-edited NMR spectroscopy

P. Tsang, M. Rance, T. M. Fieser, J. M. Ostresh, R. A. Houghten, R. A. Lerner and P. E. Wright
Biochemistry 31 (15) 3862 (1992)
https://doi.org/10.1021/bi00130a018

Proton NMR studies of [N-MeCys3,N-MeCys7]TANDEM binding to DNA oligonucleotides: sequence-specific binding at the TpA site

Kenneth J. Addess, Dara E. Gilbert, Richard K. Olsen and Juli Feigon
Biochemistry 31 (2) 339 (1992)
https://doi.org/10.1021/bi00117a005

Nuclear Magnetic Resonance Fourier Transform Spectroscopy (Nobel Lecture)

Richard R. Ernst
Angewandte Chemie International Edition in English 31 (7) 805 (1992)
https://doi.org/10.1002/anie.199208053

High-level expression of recombinant human FK-binding protein from a fusion precursor

Rohinton Edalji, Tami J. Pilot-Matias, Steven D. Pratt, David A. Egan, Jean M. Severin, Earl G. Gubbins, Andrew M. Petros, Stephen W. Fesik, Neal S. Burres and Thomas F. Holzman
Journal of Protein Chemistry 11 (3) 213 (1992)
https://doi.org/10.1007/BF01024859

Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy

Brian J. Stockman, Terrence A. Scahill, Melinda Roy, Eldon L. Ulrich, Nancy A. Strakalaitis, David P. Brunner, Anthony W. Yem and Martin R. Deibel
Biochemistry 31 (23) 5237 (1992)
https://doi.org/10.1021/bi00138a001

Sequence specific 1H‐NMR assignments and secondary structure of a carboxy‐terminal functional fragment of apolipoprotein CII

Per‐Olof LYCKSELL, Anders ÖHMAN, Gunilla BENGTSSON‐OLIVECRONA, Lennart B.‐Å. JOHANSSON, Sybren S. WIJMENGA, Dominik WERNIC and Astrid GRÄSLUND
European Journal of Biochemistry 205 (1) 223 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb16772.x

The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton‐NMR

David SIPOS, Mats ANDERSSON and Anders EHRENBERG
European Journal of Biochemistry 209 (1) 163 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17273.x

Pituitary adenylate cyclase activating polypeptide (PACAP) with 27 residues

HIROSHI INOOKA, SATOSHI ENDO, CHIEKO KITADA, EIJI MIZUTA and MASAHIKO FUJINO
International Journal of Peptide and Protein Research 40 (5) 456 (1992)
https://doi.org/10.1111/j.1399-3011.1992.tb00324.x

The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X‐ray structures

Sven G. Hyberts, Matthew S. Goldberg, Timothy F. Havel and Gerhard Wagner
Protein Science 1 (6) 736 (1992)
https://doi.org/10.1002/pro.5560010606

Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments

Timothy M. Logan, Edward T. Olejniczak, Robert X. Xu and Stephen W. Fesik
FEBS Letters 314 (3) 413 (1992)
https://doi.org/10.1016/0014-5793(92)81517-P

Homo- and heteronuclear NMR studies of the human retinoic acid receptor .beta. DNA-binding domain: sequential assignments and identification of secondary structure elements

M. Katahira, R. M. A. Knegtel, R. Boelens, D. Eib, J. G. Schilthuis, P. T. Van der Saag and R. Kaptein
Biochemistry 31 (28) 6474 (1992)
https://doi.org/10.1021/bi00143a017

Proton NMR assignments of systemin

David J. Russell, Gregory Pearce, Clarence A. Ryan and James D. Satterlee
Journal of Protein Chemistry 11 (3) 265 (1992)
https://doi.org/10.1007/BF01024865

Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints

Gaetano T. Montelione, Kurt Wuethrich, Antony W. Burgess, Edward C. Nice, Gerhard Wagner, Kenneth D. Gibson and Harold A. Scheraga
Biochemistry 31 (1) 236 (1992)
https://doi.org/10.1021/bi00116a033

Proton NMR-based determination of the secondary structure of porcine pancreatic spasmolytic polypeptide: one of a new family of "trefoil" motif containing cell growth factors

Mark D. Carr
Biochemistry 31 (7) 1998 (1992)
https://doi.org/10.1021/bi00122a015

A water-lipid interface induces a highly dynamic folded state in apocytochrome c and cytochrome c, which may represent a common folding intermediate

Harmen H. J. De Jongh, J. Antoinette Killian and Ben De Kruijff
Biochemistry 31 (6) 1636 (1992)
https://doi.org/10.1021/bi00121a008

The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

D. S. Wishart, B. D. Sykes and F. M. Richards
Biochemistry 31 (6) 1647 (1992)
https://doi.org/10.1021/bi00121a010

Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

Axel T. Brünger
Nature 355 (6359) 472 (1992)
https://doi.org/10.1038/355472a0

Membrane-bound conformation of mastoparan-X, a G-protein-activating peptide

Kaori Wakamatsu, Akihiko Okada, Tatsuo Miyazawa, Masanao Ohya and Tsutomu Higashijima
Biochemistry 31 (24) 5654 (1992)
https://doi.org/10.1021/bi00139a032

NMR studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1

Xiao Lu Zhang, Michael E. Selsted and Arthur Pardi
Biochemistry 31 (46) 11348 (1992)
https://doi.org/10.1021/bi00161a012

Folding topology of the disulfide-bonded dimeric DNA-binding domain of the myogenic determination factor MyoD

Melissa A. Starovasnik, T. Keith Blackwell, Thomas M. Laue, Harold Weintraub and Rachel E. Klevit
Biochemistry 31 (41) 9891 (1992)
https://doi.org/10.1021/bi00156a006

Solution conformation of a deoxynucleotide containing tandem G.cntdot.A mismatched base pairs and 3'-overhanging ends in d(GTGAACTT)2

Andrew Lane, Stephen R. Martin, Susanne Ebel and Tom Brown
Biochemistry 31 (48) 12087 (1992)
https://doi.org/10.1021/bi00163a018

Structural Studies of Antarctic Fish Antifreeze Glycoproteins by One- and Two-Dimensional NMR Spectroscopy

Kilian Dill, Lihua Huang, Daniel W. Bearden and Robert E. Feeney
Journal of Carbohydrate Chemistry 11 (4) 499 (1992)
https://doi.org/10.1080/07328309208017809

Conformational study of cyclo[D‐Trp‐D‐Asp‐Pro‐D‐Val‐Leu], an endothelin‐A receptor‐selective antagonist

R.Andrew Atkinson and John T. Pelton
FEBS Letters 296 (1) 1 (1992)
https://doi.org/10.1016/0014-5793(92)80390-3

NMR structural characterization of the reaction product between d(GpG) and the octahedral antitumor complex trans-RuCl2(DMSO)4

Gennaro Esposito, Sabina Cauci, Federico Fogolari, Enzo Alessio, Marco Scocchi, Franco Quadrifoglio and Paolo Viglino
Biochemistry 31 (31) 7094 (1992)
https://doi.org/10.1021/bi00146a010

Determination of the ϕ angle in a peptide backbone by NMR spectroscopy with a combination of homonuclear and heteronuclear coupling constants

Peter Schmieder and Horst Kessler
Biopolymers 32 (4) 435 (1992)
https://doi.org/10.1002/bip.360320421

The three‐dimensional structure of guanine‐specific ribonuclease F1 in solution determined by NMR spectroscopy and distance geometry

Takahisa NAKAI, Wataru YOSHIKAWA, Haruki NAKAMURA and Hiroshi YOSHIDA
European Journal of Biochemistry 208 (1) 41 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17157.x

Warum Pentose‐ und nicht Hexose‐Nucleinsäuren??. Teil II. Oligonucleotide aus 2′,3′‐Dideoxy‐β‐D‐glucopyranosyl‐Bausteinen (‘Homo‐DNS’): Herstellung.

Markus Böhringer, Hans‐JÖRg Roth, Jürg Hunziker, Michael Göbel, Ravichandran Krishnan, Alfred Giger, Bernd Schweizer, Jakob Schreiber, Christian Leumann and Albert Eschenmoser
Helvetica Chimica Acta 75 (5) 1416 (1992)
https://doi.org/10.1002/hlca.19920750503

NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1

Arthur Pardi, Xiao Lu Zhang, Michael E. Selsted, Jack J. Skalicky and Ping F. Yip
Biochemistry 31 (46) 11357 (1992)
https://doi.org/10.1021/bi00161a013

Solution conformation of human neuropeptide Y by 1H nuclear magnetic resonance and restrained molecular dynamics

Hervé DARBON, Jean‐Marie BERNASSAU, Colette DELEUZE, Jacques CHENU, Alain ROUSSEL and Christian CAMBILLAU
European Journal of Biochemistry 209 (2) 765 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17346.x

A sequence‐dependent 1H‐NMR study on the formation of β‐turns in tetrapeptides containing charged residues

Xiaohong Liu, Paul G. Scott, Albin Otter and George Kotovych
Biopolymers 32 (2) 119 (1992)
https://doi.org/10.1002/bip.360320203

Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide

F. D. Sonnichsen, J. E. Van Eyk, R. S. Hodges and B. D. Sykes
Biochemistry 31 (37) 8790 (1992)
https://doi.org/10.1021/bi00152a015

Determination of the three-dimensional structure of iberiotoxin in solution by proton nuclear magnetic resonance spectroscopy

Bruce A. Johnson and Elizabeth E. Sugg
Biochemistry 31 (35) 8151 (1992)
https://doi.org/10.1021/bi00150a006

Structure of G.cntdot.T.cntdot.A triplet in an intramolecular DNA triplex

Edmond Wang, Shiva Malek and Juli Feigon
Biochemistry 31 (20) 4838 (1992)
https://doi.org/10.1021/bi00135a015

Sequential proton NMR assignments and secondary structure of the kringle domain from urokinase

Xiang Li, Richard A. G. Smith and Christopher M. Dobson
Biochemistry 31 (40) 9562 (1992)
https://doi.org/10.1021/bi00155a008

Sequence‐specific NMR assignments of the trp repressor from Escherichia coli using three‐dimensional 15N/1H heteronuclear techniques

Katherine L. B. BORDEN, Christopher J. BAUER, Thomas A. FRENKIEL, Pamela BECKMANN and Andrew N. LANE
European Journal of Biochemistry 204 (1) 137 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb16616.x

Design and synthesis of an α‐helical peptide containing periodic proline residues

Eiichi Kitakuni, Tokio Horiuchi, Yasushi Oda, Motohisa Oobatake, Haruki Nakamura and Toshiki Tanaka
FEBS Letters 298 (2-3) 233 (1992)
https://doi.org/10.1016/0014-5793(92)80065-O

Conformations in solution of angiotensin II, and its 1–7 and 1–6 fragments

J. A. Cushman, P. K. Mishra, A. A. Bothner‐By and M. S. Khosla
Biopolymers 32 (9) 1163 (1992)
https://doi.org/10.1002/bip.360320905