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Biochemistry 32 (48) 13098 (1993)
https://doi.org/10.1021/bi00211a020

A reduced representation of proteins for use in restraint satisfaction calculations

Pawel Herzyk and Rodrick E. Hubbard
Proteins: Structure, Function, and Bioinformatics 17 (3) 310 (1993)
https://doi.org/10.1002/prot.340170308

Proton NMR resonance assignments, secondary structure, and global fold of the TR1C fragment of turkey skeletal troponin C in the calcium-free state

Wendy A. Findlay and Brian D. Sykes
Biochemistry 32 (13) 3461 (1993)
https://doi.org/10.1021/bi00064a033

Secondary structure and backbone resonance assignments of the periplasmic cyclophilin type peptidyl-prolyl isomerase from Escherichia coli

Robert T. Clubb, Venkataraman Thanabal, Jasna Fejzo, Stephen B. Ferguson, Lynne Zydowsky, C. Hunter Baker, Christopher T. Walsh and Gerhard Wagner
Biochemistry 32 (25) 6391 (1993)
https://doi.org/10.1021/bi00076a012

Sequential1H-NMR assignments of neurotoxin III from the sea anemoneHeteractis macrodactylus and structural comparison with related toxins

Mark G. Hinds and Raymond S. Norton
Journal of Protein Chemistry 12 (3) 371 (1993)
https://doi.org/10.1007/BF01028199

Conformational backbone dynamics of the cyclic decapeptide antamanide. Application of a new multiconformational search algorithm based on NMR data

M. J. Blackledge, R. Brueschweiler, C. Griesinger, J. M. Schmidt, Ping Xu and R. R. Ernst
Biochemistry 32 (41) 10960 (1993)
https://doi.org/10.1021/bi00092a005

Structural characterization of monellin in the alcohol-denatured state by NMR: Evidence for .beta.-sheet to .alpha.-helix conversion

Pei Fan, Clay Bracken and Jean Baum
Biochemistry 32 (6) 1573 (1993)
https://doi.org/10.1021/bi00057a023

The tertiary structure of a DNA aptamer which binds to and inhibits thrombin determines activity

Ke Yu Wang, Steven H. Krawczyk, Norbert Bischofberger, S. Swaminathan and Philip H. Bolton
Biochemistry 32 (42) 11285 (1993)
https://doi.org/10.1021/bi00093a004

A single-stranded amphipathic .alpha.-helix in aqueous solution: Design, structural characterization, and its application for determining .alpha.-helical propensities of amino acids

Nian E. Zhou, Cyril M. Kay, Brian D. Sykes and Robert S. Hodges
Biochemistry 32 (24) 6190 (1993)
https://doi.org/10.1021/bi00075a011

Recombinant human IL-6 expressed inE. coli undergoes selective N-terminal degradation: Evidence that the protein consists of a stable core and a nonessential flexible N-terminal

Amanda E. I. Proudfoot, Steven C. Brown, Alain R. Bernard, Jean-Yves Bonnefoy and Eric H. Kawashima
Journal of Protein Chemistry 12 (4) 489 (1993)
https://doi.org/10.1007/BF01025050