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:

A1H and13C NMR Study on the Role of Salt-Bridges in the Formation of a Type I β-Turn in N-Acetyl-L-Asp-L-Glu-L-Lys-L-Ser-NH2

Albin Otter, Paul G. Scott, Xiaohong Liu and George Kotovych
Journal of Biomolecular Structure and Dynamics 7 (3) 455 (1989)
https://doi.org/10.1080/07391102.1989.10508504

Overcoming the overlap problem in the assignment of proton NMR spectra of larger proteins by use of three-dimensional heteronuclear proton-nitrogen-15 Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1.beta.

Dominique Marion, Paul C. Driscoll, Lewis E. Kay, Paul T. Wingfield, Ad Bax, Angela M. Gronenborn and G. Marius Clore
Biochemistry 28 (15) 6150 (1989)
https://doi.org/10.1021/bi00441a004

Electrostatic interactions in wild-type and mutant recombinant human myoglobins

Raghavan Varadarajan, David G. Lambright and Steven G. Boxer
Biochemistry 28 (9) 3771 (1989)
https://doi.org/10.1021/bi00435a022

Sequence Determination of a Tetrapeptide Using Long‐Rang Heteronuclear Shift Correlation 2D NMR Spectroscopy

Fong‐Ku Shi, Ying‐Chih Lin and Kung‐Tsung Wang
Journal of the Chinese Chemical Society 36 (5) 423 (1989)
https://doi.org/10.1002/jccs.198900058

Ein chemischer Weg zu neuen Proteinen – Templat‐assoziierte synthetische Proteine (TASP)

Manfred Mutter and Stéphane Vuilleumier
Angewandte Chemie 101 (5) 551 (1989)
https://doi.org/10.1002/ange.19891010504

Two-Dimensional1H and31P NMR Spectra of a Decamer Oligodeoxyribonucleotide Duplex and a Quinoxaline ([MeCys3, MeCys7]TANDEM) Drug Duplex Complex

Robert Powers, Richard K. Olsen and David G. Gorenstein
Journal of Biomolecular Structure and Dynamics 7 (3) 515 (1989)
https://doi.org/10.1080/07391102.1989.10508507

Two‐dimensional 1H‐NMR study of the 1–34 fragment of human parathyroid hormone

Susannie C. Lee and Anne F. Russell
Biopolymers 28 (6) 1115 (1989)
https://doi.org/10.1002/bip.360280606

Two‐dimensional 1H‐nmr study of synthetic peptides containing the main immunogenic region of the Torpedo acetylcholine receptor

M. T. Cung, M. Marraud, I. Hadjidakis, E. Bairaktari, C. Sakarellos, A. Kokla and S. Tzartos
Biopolymers 28 (1) 465 (1989)
https://doi.org/10.1002/bip.360280141

Conformational analysis of cyclic peptides in solution

Horst Kessler, Jan‐Willem Bats, Klaus Wagner and Martin Will
Biopolymers 28 (1) 385 (1989)
https://doi.org/10.1002/bip.360280136

Synthèse d'une sonde biotinylée à bras clivable allongé pour l'isolement des récepteurs de l'angiotensine II

René Seyer, André Aumelas, Jacky Marie, Jean Claude Bonnafous and Serge Jard
Helvetica Chimica Acta 72 (4) 678 (1989)
https://doi.org/10.1002/hlca.19890720409

Labaditin, a novel cyclic decapeptide from the latex of Jatropha multifida L. (Euphorbiaceae)

S. Kosasi, W.G. van der Sluis, R. Boelens, L.A.'t Hart and R.P. Labadie
FEBS Letters 256 (1-2) 91 (1989)
https://doi.org/10.1016/0014-5793(89)81724-7

Proton NMR studies of bovine and porcine phospholipase A2: assignment of aromatic resonances and evidence for a conformational equilibrium in solution

J. Fisher, W. U. Primrose, G. C. K. Roberts, N. Dekker, R. Boelens, R. Kaptein and A. J. Slotboom
Biochemistry 28 (14) 5939 (1989)
https://doi.org/10.1021/bi00440a034

Multinuclear NMR studies of DNA hairpins. 1. Structure and dynamics of d(CGCGTTGTTCGCG)

James R. Williamson and Steven G. Boxer
Biochemistry 28 (7) 2819 (1989)
https://doi.org/10.1021/bi00433a012

A powerful method of sequential proton resonance assignment in proteins using relayed 15N‐1H multiple quantum coherence spectroscopy

Angela M. Gronenborn, Ad Bax, Paul T. Wingfield and G.Marius Clore
FEBS Letters 243 (1) 93 (1989)
https://doi.org/10.1016/0014-5793(89)81224-4

A structural study of phosphate‐methylated d(CpG)n and d(GpC)n DNA oligomers. Implications of phosphate shielding for the isomerisation of B‐DNA into Z‐DNA

Peter J. L. M. Quaedflieg, Leo H. Koole, Marcel H. P. van Genderen and Henk M. Buck
Recueil des Travaux Chimiques des Pays-Bas 108 (11) 421 (1989)
https://doi.org/10.1002/recl.19891081107

Conformational behavior of cyclic CCK‐related peptides determined by 400‐MHz 1H‐nmr: Relationships with affinity and selectivity for brain receptors

P. Roy, B. Charpentier, C. Durieux, A. Dor and B. P. Roques
Biopolymers 28 (1) 69 (1989)
https://doi.org/10.1002/bip.360280110

High-resolution NMR studies of fibrinogen-like peptides in solution: structure of a thrombin-bound peptide corresponding to residues 7-16 of the A.alpha. chain of human fibrinogen

Feng Ni, Yvonne C. Meinwald, Max Vasquez and Harold A. Scheraga
Biochemistry 28 (7) 3094 (1989)
https://doi.org/10.1021/bi00433a053

The sequence‐specific assignment of the 1H‐NMR spectrum of an enzyme, horse‐muscle acylphosphatase

Vladimir SAUDEK, Jonathan BOYD, Robert J. P. WILLIAMS, Massimo STEFANI and Giampietro RAMPONI
European Journal of Biochemistry 182 (1) 85 (1989)
https://doi.org/10.1111/j.1432-1033.1989.tb14803.x

Preliminary assignments of the aromatic and some methyl group resonances of the 1H‐NMR spectrum of the oxidized form of uteroglobin

Nadège JAMIN, Pierre ROY, Françoise FRIDLANSKY, Muriel DELEPIERRE, Edwin MILGROM, Bernard P. ROQUES and Jean‐Paul MORNON
European Journal of Biochemistry 183 (1) 219 (1989)
https://doi.org/10.1111/j.1432-1033.1989.tb14916.x

1H n.m.r. conformational studies on the C‐terminal octapeptide of oxyntomodulin, a β‐turn locked by a salt bridge

ANDRÉ AUMELAS, MARIE‐PASCALE AUDOUSSET‐PUECH, ANNIE HEITZ, DOMINIQUE BATAILLE and JEAN MARTINEZ
International Journal of Peptide and Protein Research 34 (4) 268 (1989)
https://doi.org/10.1111/j.1399-3011.1989.tb01574.x

Magnetization‐transfer n.m.r. investigation of the hydrogen exchang in H20 of the peptide fragment B23‐B29 of insulin

FRITS ABILDGAARD, JENS J. LED, PER BALSCHMIDT and FINN B. HANSEN
International Journal of Peptide and Protein Research 34 (4) 340 (1989)
https://doi.org/10.1111/j.1399-3011.1989.tb01584.x

Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor

Mark C. Manning and Robert W. Woody
Biochemistry 28 (21) 8609 (1989)
https://doi.org/10.1021/bi00447a051

Peptidkonformationen, 50. Synthese und Konformationsanalyse von cyclischen Alanin‐Analogen des Thymopoietins durch NMR‐Spektroskopie und Molecular‐Dynamics‐Rechnungen im Vakuum und in Lösung

Horst Kessler, Armin G. Klein, Rainer Obermeier and Martin Will
Liebigs Annalen der Chemie 1989 (3) 269 (1989)
https://doi.org/10.1002/jlac.198919890150

Intrauterine fetal brain NMR spectroscopy: 1H and 31P studies in rats

Tsutomu Nakada, Ingrid L. Kwee, Nobuyuki Suzuki and Kiyohiro Houkin
Magnetic Resonance in Medicine 12 (2) 172 (1989)
https://doi.org/10.1002/mrm.1910120204

Conformations of dehydrophenylalanine containing peptides: nmr studies of an acyclic hexapeptide with two Δz‐Phe residues

V. S. Chauhan, K. Uma, Paramjeet Kaur and P. Balaram
Biopolymers 28 (3) 763 (1989)
https://doi.org/10.1002/bip.360280306

Optimising selective deuteration of proteins for 2D 1H NMR detection and assignment studies Application to the Phe residues of Lactobacillus casei dihydrofolate reductase

J. Feeney, B. Birdsall, J. Akiboye, S.J.B. Tendler, J.Jiménez Barbero, G. Ostler, J.R.P. Arnold, G.C.K. Roberts, A. Kühn and K. Roth
FEBS Letters 248 (1-2) 57 (1989)
https://doi.org/10.1016/0014-5793(89)80431-4

Three‐dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy

Hans Widmer, Martin Billeter and Kurt Wüthrich
Proteins: Structure, Function, and Bioinformatics 6 (4) 357 (1989)
https://doi.org/10.1002/prot.340060403

Observation of a tight‐turn conformation in a proline‐containing inhibitor of renin angiotensin

Sudha Srivastava, Ratna S. Phadke and Girjesh Govil
Magnetic Resonance in Chemistry 27 (5) 455 (1989)
https://doi.org/10.1002/mrc.1260270507

A Chemical Approach to Protein Design—Template‐Assembled Synthetic Proteins (TASP)

Manfred Mutter and Stéphane Vuilleumier
Angewandte Chemie International Edition in English 28 (5) 535 (1989)
https://doi.org/10.1002/anie.198905353

NMR studies of triple-strand formation from the homopurine-homopyrimidine deoxyribonucleotides d(GA)4 and d(TC)4

Ponni Rajagopal and Juli Feigon
Biochemistry 28 (19) 7859 (1989)
https://doi.org/10.1021/bi00445a048

The influence of stereospecific assignments on the determination of three‐dimensional structures of proteins by nuclear magnetic resonance spectroscopy

Paul C. Driscoll, Angela M. Gronenborn and G.Marius Clore
FEBS Letters 243 (2) 223 (1989)
https://doi.org/10.1016/0014-5793(89)80134-6

Concerted two-dimensional NMR approaches to hydrogen-1, carbon-13, and nitrogen-15 resonance assignments in proteins

Brian J. Stockman, Michael D. Reily, William M. Westler, Eldon L. Ulrich and John L. Markley
Biochemistry 28 (1) 230 (1989)
https://doi.org/10.1021/bi00427a032

NMR assignments for the amino-terminal residues of trp repressor and their role in DNA binding

Cheryl H. Arrowsmith, Jannette Carey, Lynda Treat-Clemons and Oleg Jardetzky
Biochemistry 28 (9) 3875 (1989)
https://doi.org/10.1021/bi00435a037

Solution structures of .alpha.-conotoxin G1 determined by two-dimensional NMR spectroscopy

Arthur Pardi, Alphonse Galdes, James Florance and Duane Maniconte
Biochemistry 28 (13) 5494 (1989)
https://doi.org/10.1021/bi00439a026

Complete assignment of the deoxyribose 5'/5" proton resonances of the EcoRI DNA sequence using isotropic mixing

Steffen J. Glaser, M. Lyndsay Remerowski and Gary P. Drobny
Biochemistry 28 (4) 1483 (1989)
https://doi.org/10.1021/bi00430a009

Two-dimensional proton and phosphorus-31 NMR spectra and restrained molecular dynamics structure of an extrahelical adenosine tridecamer oligodeoxyribonucleotide duplex

Edward Nikonowicz, Vikram Roongta, Claude R. Jones and David G. Gorenstein
Biochemistry 28 (22) 8714 (1989)
https://doi.org/10.1021/bi00448a007

Mobility of secondary structure units of horse‐muscle acylphosphatase

Vladimir SAUDEK, Robert J. P. WILLIAMS, Massimo STEFANI and Giampietro RAMPONI
European Journal of Biochemistry 185 (1) 99 (1989)
https://doi.org/10.1111/j.1432-1033.1989.tb15087.x

Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution

Andrew D. Robertson, Enrico O. Purisima, Margaret A. Eastman and Harold A. Scheraga
Biochemistry 28 (14) 5930 (1989)
https://doi.org/10.1021/bi00440a033

Conformational Analysis of Didemnins. A multidisciplinary approach by means of X‐Ray, NMR, molecular‐dynamics, and molecular‐mechanics techniques

Horst Kessler, Martin Will, Jochen Antel, Holger Beck and George M. Sheldrick
Helvetica Chimica Acta 72 (3) 530 (1989)
https://doi.org/10.1002/hlca.19890720316

Improved strategies for the determination of protein structures from NMR data: The solution structure of acyl carrier protein

T.A. Holak, M. Nilges and H. Oschkinat
FEBS Letters 242 (2) 218 (1989)
https://doi.org/10.1016/0014-5793(89)80473-9

Stereospecific assignment of the methyl 1H NMR lines of valine and leucine in polypeptides by nonrandom 13C labelling

H. Senn, B. Werner, B.A. Messerle, C. Weber, R. Traber and K. Wüthrich
FEBS Letters 249 (1) 113 (1989)
https://doi.org/10.1016/0014-5793(89)80027-4

A proton nuclear magnetic resonance study on the solution structure of crotamine

Toshiya Endo, Masanao Oya, Hiroshi Ozawa, Yoshio Kawano, José R. Giglio and Tatsuo Miyazawa
Journal of Protein Chemistry 8 (6) 807 (1989)
https://doi.org/10.1007/BF01024904

1H‐NMR study of endothelin, sequence‐specific assignment of the spectrum and a solution structure

Vladimir Saudek, Jan Hoflack and John T. Pelton
FEBS Letters 257 (1) 145 (1989)
https://doi.org/10.1016/0014-5793(89)81807-1

The structure and properties of horse muscle acylphosphatase in solution Mobility of antigenic and active site regions

Vladimir Saudek, Robert J.P. Williams and Giampietro Ramponi
FEBS Letters 242 (2) 225 (1989)
https://doi.org/10.1016/0014-5793(89)80474-0

Proton and Phosphorus NMR Study of RNA Self-Complementary Hexamers: Influence of the 5-Methylcytidine on the Conformational Transitions and the Molecular Motions

G. Bloch, F. Ceolin, F. Macquaire, J. M. Neumann, F. Babin and T. Huynh-Dinh
Journal of Biomolecular Structure and Dynamics 6 (6) 1151 (1989)
https://doi.org/10.1080/07391102.1989.10506542

Solution conformation of endothelin determined by nuclear magnetic resonance and distance geometry

Satoshi Endo, Hiroshi Inooka, Yoshihiro Ishibashi, Chieko Kitada, Eiji Mizuta and Masahiko Fujino
FEBS Letters 257 (1) 149 (1989)
https://doi.org/10.1016/0014-5793(89)81808-3

Proton‐detected C,H correlation NMR techniques for the complete assignment of all proton and carbon resonances of a cyclic peptide

Mechtild Hofmann, Matthias Gehrke, Wolfgang Bermel and Horst Kessler
Magnetic Resonance in Chemistry 27 (9) 877 (1989)
https://doi.org/10.1002/mrc.1260270911

Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a

Erik R. P. Zuiderweg and Stephen W. Fesik
Biochemistry 28 (6) 2387 (1989)
https://doi.org/10.1021/bi00432a008

The effects of multiple amino acid substitutions on the polypeptide backbone of tuna and horse cytochromes c

Yuan GAO, A. Daniel J. LEE, Robert J. P. WILLIAMS and Glyn WILLIAMS
European Journal of Biochemistry 182 (1) 57 (1989)
https://doi.org/10.1111/j.1432-1033.1989.tb14800.x

Solution conformation of a synthetic fragment of human pituitary growth hormone. Two-dimensional NMR of an .alpha.-helical dimer

Vikram Roongta, Robert Powers, Claude Jones, Michael J. Beakage, James E. Shields and David G. Gorenstein
Biochemistry 28 (3) 1048 (1989)
https://doi.org/10.1021/bi00429a019

Static and transient hydrogen-bonding interactions in recombinant desulfatohirudin studied by proton nuclear magnetic resonance measurements of amide proton exchange rates and pH-dependent chemical shifts

Hideyuki Haruyama, Yan Qiu Qian and Kurt Wuethrich
Biochemistry 28 (10) 4312 (1989)
https://doi.org/10.1021/bi00436a028

Limited sampling of conformational space by the distance geometry algorithm: implications for structures generated from NMR data

William J. Metzler, Dennis R. Hare and Arthur Pardi
Biochemistry 28 (17) 7045 (1989)
https://doi.org/10.1021/bi00443a040

Determination of Three-Dimensional Structures of Proteins and Nucleic Acids in Solution by Nuclear Magnetic Resonance Spectroscop

G. Marius Clore and Angela M. Gronenborn
Critical Reviews in Biochemistry and Molecular Biology 24 (5) 479 (1989)
https://doi.org/10.3109/10409238909086962

A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin

Julie D. Forman-Kay, G. Marius Clore, Paul C. Driscoll, Paul Wingfield, Frederic M. Richards and Angela M. Gronenborn
Biochemistry 28 (17) 7088 (1989)
https://doi.org/10.1021/bi00443a045

NMR studies of the influence of dodecyl sulfate on the amide hydrogen exchange kinetics of a micelle-solubilized hydrophobic tripeptide

Joe D. J. O'Neil and Brian D. Sykes
Biochemistry 28 (2) 699 (1989)
https://doi.org/10.1021/bi00428a043

Analysis of the relative contributions of the nuclear Overhauser interproton distance restraints and the empirical energy function in the calculation of oligonucleotide structures using restrained molecular dynamics

Angela M. Gronenborn and G. Marius Clore
Biochemistry 28 (14) 5978 (1989)
https://doi.org/10.1021/bi00440a039

Conformation of recombinant desulfatohirudin in aqueous solution determined by nuclear magnetic resonance

Hideyuki Haruyama and Kurt Wuethrich
Biochemistry 28 (10) 4301 (1989)
https://doi.org/10.1021/bi00436a027

Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing

Per J. Kraulis, G. Marius Clore, Michael Nilges, T. Alwyn Jones, Goeran Pettersson, Jonathan Knowles and Angela M. Gronenborn
Biochemistry 28 (18) 7241 (1989)
https://doi.org/10.1021/bi00444a016

Sequential 1H‐NMR assignment and solution structure of bovine pancreatic ribonuclease A

Manuel RICO, Marta BRUIX, Jorge SANTORO, Carlos GONZALEZ, José Luis NEIRA, José Luis NIETO and José HERRANZ
European Journal of Biochemistry 183 (3) 623 (1989)
https://doi.org/10.1111/j.1432-1033.1989.tb21092.x

Conformational studies of d(AAAAATTTTT)2 using constraints from nuclear Overhauser effects and from quantitative analysis of the cross-peak fine structures in two-dimensional proton nuclear magnetic resonance spectra

Bernardo Celda, Hans Widmer, Werner Leupin, Walter J. Chazin, William A. Denny and Kurt Wuethrich
Biochemistry 28 (4) 1462 (1989)
https://doi.org/10.1021/bi00430a006

A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure

Paul C. Driscoll, G. Marius Clore, Laszlo Beress and Angela M. Gronenborn
Biochemistry 28 (5) 2178 (1989)
https://doi.org/10.1021/bi00431a032

Investigation of the solution structures and mobility of oxidised and reduced cytochrome b5 by 2D NMR spectroscopy

Nigel C. Veitch, David W. Concar, Robert J.P. Williams and David Whitford
FEBS Letters 238 (1) 49 (1988)
https://doi.org/10.1016/0014-5793(88)80223-0

A proton nuclear magnetic resonance study of the conformation of bovine anaphylatoxin C5a in solution

Jutta Zarbock, Renato Gennaro, Domenico Romeo, G.Marius Clore and Angela M. Gronenborn
FEBS Letters 238 (2) 289 (1988)
https://doi.org/10.1016/0014-5793(88)80499-X

High-Field NMR and Circular Dichroism Solvent-Dependent Conformational Studies of the Bradykinin C-Terminal Tetrapeptide Ser-Pro-Phe-Arg

Albin Otter, Paul G. Scott, John R. Cann, Raymond J. Vavrek, John M. Stewart and George Kotovych
Journal of Biomolecular Structure and Dynamics 6 (3) 609 (1988)
https://doi.org/10.1080/07391102.1988.10506511

2D NMR investigation of the binding of the anticancer drug actinomycin D to duplexed dATGCGCAT: conformational features of the unique 2:1 adduct

Elwood V. Scott, Gerald Zon, Luigi G. Marzilli and W. David Wilson
Biochemistry 27 (20) 7940 (1988)
https://doi.org/10.1021/bi00420a053

Type I collagen .alpha.-1 chain C-telopeptide: solution structure determined by 600-MHz proton NMR spectroscopy and implications for its role in collagen fibrillogenesis

Albin Otter, Paul G. Scott and George Kotovych
Biochemistry 27 (10) 3560 (1988)
https://doi.org/10.1021/bi00410a006

Methionine-90-spin-labeled bovine .alpha.-lactalbumin: electron spin resonance and NMR distance measurements

Giovanni Musci, Keiko Koga and Lawrence J. Berliner
Biochemistry 27 (4) 1260 (1988)
https://doi.org/10.1021/bi00404a028

Zweidimensionale NMR‐Spektroskopie, Grundlagen und Übersicht über die Experimente

Horst Kessler, Matthias Gehrke and Christian Griesinger
Angewandte Chemie 100 (4) 507 (1988)
https://doi.org/10.1002/ange.19881000407

Atomic Motions in Molecular Crystals from Diffraction Measurements

Jack D. Dunitz, Emily F. Maverick and Kenneth N. Trueblood
Angewandte Chemie International Edition in English 27 (7) 880 (1988)
https://doi.org/10.1002/anie.198808801

Long‐range 15N‐1H correlation as an aid to sequential proton resonance assignment of proteins Application to the DNA‐binding protein ner from phage Mu

G.Marius Clore, Ad Bax, Paul Wingfield and Angela M. Gronenborn
FEBS Letters 238 (1) 17 (1988)
https://doi.org/10.1016/0014-5793(88)80216-3

Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR

Heinrich Roder, Gülnur A. Elöve and S. Walter Englander
Nature 335 (6192) 700 (1988)
https://doi.org/10.1038/335700a0

Determination of three‐dimensional structures of proteins from interproton distance data by hybrid distance geometry‐dynamical simulated annealing calculations

Michael Nilges, G.Marius Clore and Angela M. Gronenborn
FEBS Letters 229 (2) 317 (1988)
https://doi.org/10.1016/0014-5793(88)81148-7

NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A

Jayant B. Udgaonkar and Robert L. Baldwin
Nature 335 (6192) 694 (1988)
https://doi.org/10.1038/335694a0

Selective reversible deuteriation of oligodeoxynucleotides: simplification of two-dimensional nuclear Overhauser effect NMR spectral assignment of a non-self-complementary dodecamer duplex

Charles K. Brush, Michael P. Stone and Thomas M. Harris
Biochemistry 27 (1) 115 (1988)
https://doi.org/10.1021/bi00401a019

Two‐dimensional 1H‐NMR study of bacterioopsin‐(34–65)‐polypeptide conformation

Alexander S. Arseniev, Innokenti V. Maslennikov, Vladimir F. Bystrov, Alexander T. Kozhich, Vadim T. Ivanov and Yuri A. Ovchinnikov
FEBS Letters 231 (1) 81 (1988)
https://doi.org/10.1016/0014-5793(88)80707-5

Structure and Reactivity of Lithium Enolates. From Pinacolone to Selective C‐Alkylations of Peptides. Difficulties and Opportunities Afforded by Complex Structures

Dieter Seebach
Angewandte Chemie International Edition in English 27 (12) 1624 (1988)
https://doi.org/10.1002/anie.198816241

Analysis of intrasugar interproton NOESY cross‐peaks as an aid to determine sugar geometries in DNA fragments

K.V.R. Chary and Sandeep Modi
FEBS Letters 233 (2) 319 (1988)
https://doi.org/10.1016/0014-5793(88)80451-4

Secondary structure of the human growth hormone releasing factor (GRF 1–29) by two‐dimensional 1H‐nmr spectroscopy

Y. Theriault, Y. Boulanger and J. K. Saunders
Biopolymers 27 (12) 1897 (1988)
https://doi.org/10.1002/bip.360271204

High-resolution NMR studies of fibrinogen-like peptides in solution: resonance assignments and conformational analysis of residues 1-23 of the A.alpha. chain of human fibrinogen

Feng Ni, Harold A. Scheraga and Susan T. Lord
Biochemistry 27 (12) 4481 (1988)
https://doi.org/10.1021/bi00412a040

Mobile sequences in the pyruvate dehydrogenase complex, the E2 component, the catalytic domain and the 2‐oxoglutarate dehydrogenase complex of Azotobacter vinelandii, as detected by 600 MHz 1H‐NMR spectroscopy

Roeland Hanemaaijer, Jacques Vervoort, Adrie H. Westphal, Arie de Kok and Cees Veeger
FEBS Letters 240 (1-2) 205 (1988)
https://doi.org/10.1016/0014-5793(88)80369-7

Indirect two‐dimensional heteronuclear NMR spectroscopy of low‐γ metal nuclei (M = 183W, 57Fe, 103Rh, 61Ni)

Reinhard Benn and Anna Rufińska
Magnetic Resonance in Chemistry 26 (10) 895 (1988)
https://doi.org/10.1002/mrc.1260261015

Solution structure of apamin determined by nuclear magnetic resonance and distance geometry

Joseph H. B. Pease and David E. Wemmer
Biochemistry 27 (22) 8491 (1988)
https://doi.org/10.1021/bi00422a029

Extraction of 1H1H and 1H13C dipolar couplings from spectra acquired in inhomogeneous magnetic fields

Lewis E. Kay, D. S. Thomson and J. H. Prestegard
Magnetic Resonance in Chemistry 26 (10) 860 (1988)
https://doi.org/10.1002/mrc.1260261010

One‐ and two‐dimensional NMR investigations of the heme pocket in free α(CO) chains from human hemoglobin

Corinne SCHAEFFER, Constantin T. CRAESCU, Joël MISPELTER, Marie‐Claude GAREL, Jean ROSA and Jean‐Marc LHOSTE
European Journal of Biochemistry 173 (2) 317 (1988)
https://doi.org/10.1111/j.1432-1033.1988.tb14001.x