A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis

Kendrew, J. C.; Bodo, G.; Dintzis, Howard M.; Parrish, R. G.; Wyckoff, Harold W.; Phillips, David

doi:10.1038/181662a0

Cited by 1,367 publications

(794 citation statements)

References 7 publications

Supporting

Mentioning

755

Contrasting

Unclassified

Order By: Relevance

“…This intuition was confirmed by the first protein structure showing that hydrophobic residues are indeed preferentially buried in the protein interior (Kendrew et al, 1958). Walter Kauzmann introduced the term 'hydrophobic bonding' to describe interactions driven by exclusion from water (Kauzmann, 1959).…”

Section: Hydrophobicitymentioning

confidence: 93%

Computational analyses of the surface properties of protein–protein interfaces

Gruber

Zawaira

Saunders

et al. 2006

Acta Crystallogr D Biol Crystallogr

View full text Add to dashboard Cite

Several potential applications of structural biology depend on discovering how one macromolecule might recognize a partner. Experiment remains the best way to answer this question, but computational tools can contribute where this fails. In such cases, structures may be studied to identify patches of exposed residues that have properties common to interaction surfaces and the locations of these patches can serve as the basis for further modelling or for further experimentation. To date, interaction surfaces have been proposed on the basis of unusual physical properties, unusual propensities for particular amino-acid types or an unusually high level of sequence conservation. Using the CXXSurface toolkit, developed as a part of the CCP4MG program, a suite of tools to analyse the properties of surfaces and their interfaces in complexes has been prepared and applied. These tools have enabled the rapid analysis of known complexes to evaluate the distribution of (i) hydrophobicity, (ii) electrostatic complementarity and (iii) sequence conservation in authentic complexes, so as to assess the extent to which these properties may be useful indicators of probable biological function.

show abstract

Section: Hydrophobicitymentioning

confidence: 93%

Computational analyses of the surface properties of protein–protein interfaces

Gruber

Zawaira

Saunders

et al. 2006

Acta Crystallogr D Biol Crystallogr

View full text Add to dashboard Cite

show abstract

“…Their recommendations are the basis of an on-going research program to develop methods and software for 3DEM validation. Early structures included myoglobin (1 PDB ID 1mbn [6,7]), the first structure solved by X-ray crystallography, and small enzymes (2 top 4pti [48], bottom right 2cha [49], bottom left 3cpa [50]). As technologies developed, the archive grew to host examples of tRNA (3 6tna [51]), viruses (4 4rhv [52]), antibodies (5 1igt [53]), protein-DNA complexes (6 top to bottom, 1gdt [54], 1tro [55], 2bop [56], 1aoi [57]), ribosomes (7 1fjg, 1fka, 1ffk [58][59][60]), and chaperones (8 1aon [61])…”

Section: Validationmentioning

confidence: 99%

“…Both Hodgkin and Perutz trained large numbers of crystallographers who set up laboratories around the world. John Kendrew arrived at Cambridge's newly formed Medical Research Council Laboratory of Molecular Biology and determined the structure of myoglobin in 1957 [6,7]. He went on to found the European Molecular Biology Laboratory.…”

mentioning

confidence: 99%

The Protein Data Bank archive as an open data resource

Berman

Kleywegt

Nakamura

et al. 2014

J Comput Aided Mol Des

117

View full text Add to dashboard Cite

show abstract

“…Sperm whale Mb was the first protein of which the three-dimensional structure was revealed by X-ray crystallography [9]. The structure of human Hb followed five years later [10].…”

Section: Introductionmentioning

confidence: 99%

Exploring three different expression systems for recombinant expression of globins: Escherichia coli, Pichia pastoris and Spodoptera frugiperda

Bracke

Hoogewijs

Dewilde

2018

Analytical Biochemistry

View full text Add to dashboard Cite

A B S T R A C TGlobins are among the best investigated proteins in biological and medical sciences and represent a prime tool for the study of the evolution of genes and the structure-function relationship of proteins. Here, we explore the recombinant expression of globins in three different expression systems: Escherichia coli, Pichia pastoris and the baculovirus infected Spodoptera frugiperda. We expressed two different human globin types in these three expression systems: I) the well-characterized neuroglobin and II) the uncharacterized, circular permutated globin domain of the large chimeric globin androglobin. It is clear from the literature that E.coli is the most used expression system for expression and purification of recombinant globins. However, the major disadvantage of E. coli is the formation of insoluble aggregates. We experienced that, for more complex multi-domain globins, like the chimeric globin androglobin, it is recommended to switch to a higher eukaryotic expression system.

show abstract

A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis

Cited by 1,367 publications

References 7 publications

Computational analyses of the surface properties of protein–protein interfaces

Computational analyses of the surface properties of protein–protein interfaces

The Protein Data Bank archive as an open data resource

Exploring three different expression systems for recombinant expression of globins: Escherichia coli, Pichia pastoris and Spodoptera frugiperda

Contact Info

Product

Resources

About