(Q27639826)

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Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography

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Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography (English)

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X-ray crystallography

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1 reference

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inferred from title

object named as

Xinhua Ji

8

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Andrey V Kajava

6

object named as

Andrey V Kajava

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author name string

Ruiai Chu

1

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Jiro Takei

2

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J Randolph Knowlton

3

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Michelle Andrykovitch

4

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Wuhong Pei

5

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Peter J Steinbach

7

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Yawen Bai

9

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language of work or name

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publication date

18 October 2002

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Journal of Molecular Biology

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323

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2

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253-62

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De novo design and structural characterization of proteins and metalloproteins

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Core-directed protein design

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Solution structure and dynamics of a de novo designed three-helix bundle protein

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De novo protein design: fully automated sequence selection

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A designed four helix bundle protein with native-like structure

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De novo design of fibrils made of short alpha-helical coiled coil peptides

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Functionalization of designed folded polypeptides

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Effect of four helix bundle topology on heme binding and redox properties

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Design, structure and stability of a hyperthermophilic protein variant

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Crystallization of a designed peptide from a molten globule ensemble

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A designed heterotrimeric coiled coil

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De novo design of native proteins: characterization of proteins intended to fold into antiparallel, rop-like, four-helix bundles.

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A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil

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A new approach to the design of uniquely folded thermally stable proteins

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Core-directed protein design. I. An experimental method for selecting stable proteins from combinatorial libraries

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Core-directed protein design. II. Rescue of a multiply mutated and destabilized variant of ubiquitin

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Searching for Peptide Ligands with an Epitope Library

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Proteolytic selection for protein folding using filamentous bacteriophages

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Selecting proteins with improved stability by a phage-based method

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In-vitro selection of highly stabilized protein variants with optimized surface

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Novel folded protein domains generated by combinatorial shuffling of polypeptide segments

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Solution structure of apocytochrome b562

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A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range

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Effect of heme binding on the structure and stability of Escherichia coli apocytochrome b562

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How do small single-domain proteins fold?

1 reference

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Primary structure effects on peptide group hydrogen exchange

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Lack of definable nucleation sites in the rate-limiting transition state of barnase under native conditions

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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NMR View: A computer program for the visualization and analysis of NMR data

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Processing of X-ray diffraction data collected in oscillation mode

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Improvement of the 2.5 A resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics

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Electron-density map interpretation

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The solution structure of oxidized Escherichia coli cytochrome b562

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The C Terminus of Apocytochrome b562 Undergoes Fast Motions and Slow Exchange among Ordered Conformations Resembling the Folded State

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Raster3D: photorealistic molecular graphics

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Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure

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Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein

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Hydrogen Exchange in Proteins

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10.1016/S0022-2836(02)00884-7

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