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D.M. Blow

Bio: D.M. Blow is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Side chain & Crystallographic point group. The author has an hindex of 12, co-authored 13 publications receiving 2222 citations.

Papers
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Journal ArticleDOI
TL;DR: In this article, Rossmann and Blow describe how they have detected the existence of partial, approximate symmetry from a knowledge of the intensities alone, and the effect of noncrystallographic symmetry, whether partial or total, results in decreasing the size of the structure to be determined, while the number of observable intensities remains the same.
Abstract: In this paper, Rossmann & Blow describe how they have detected the existence of partial, approximate symmetry from a knowledge of the intensities alone. The effect of noncrystallographic symmetry, whether partial or total, results in decreasing the size of the structure to be determined, while the number of observable intensities remains the same.

863 citations

Journal ArticleDOI
TL;DR: Refined atomic co-ordinates for tosyl-α-chymotrypsin have been obtained by computational refinement of co-coordinates derived from a carefully built atomic model as mentioned in this paper.

614 citations

Journal ArticleDOI
TL;DR: A detailed analysis of the binding of N-formyl-l-tryptophan to the active site of α-chymotrypsin shows that the indolyl side chain lies in a hydrophobic pocket or slit, which accounts for the specificity of this enzyme for binding arginine or lysine side chains.

350 citations

Journal ArticleDOI
TL;DR: In this article, the positions and orientations of the inhibitor groups were determined from difference Fourier projections calculated using phase angles derived from a single isomorphous heavy-atom derivative.

71 citations


Cited by
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Journal ArticleDOI
15 Aug 1970-Nature
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Abstract: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products. Four major components of the head are cleaved during the process of assembly, apparently after the precursor proteins have assembled into some large intermediate structure.

232,912 citations

Journal Article
01 Jan 1970-Nature
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Abstract: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products. Four major components of the head are cleaved during the process of assembly, apparently after the precursor proteins have assembled into some large intermediate structure.

203,017 citations

Journal ArticleDOI
16 Jul 1992-Nature
TL;DR: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 Å and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serumalbumin.
Abstract: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 A. It comprises three homologous domains that assemble to form a heart-shaped molecule. Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. The structure explains numerous physical phenomena and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serum albumin.

3,482 citations

Book
01 Jan 1992
TL;DR: This manual to X-PLOR Version 3.1 presents the theoretical background, syntax and function of the programme and also provides a comprehensive list of references and sample input files with comments.
Abstract: X-PLOR is a highly sophisticated computer program that provides an interface between theoretical foundations and experimental data in structural biology, with specific emphasis on X-ray crystallography and nuclear magnetic resonance spectroscopy in solution of large biological macro-molecules. This manual to X-PLOR Version 3.1 presents the theoretical background, syntax, and function of the program and also provides a comprehensive list of references and sample input files with comments. It is intended primarily for researchers and students in the fields of computational chemistry, structural biology, and computational molecular biology.

3,449 citations

Journal ArticleDOI

3,212 citations