World's Best Scientists 2026 revealed!
Michael P. Williamson

Michael P. Williamson

D-Index & Metrics

Chemistry

D-Index
78
Citations
24917
World Ranking
3751
National Ranking
215

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Amino acid
  • Biochemistry

Michael P. Williamson focuses on Biochemistry, Binding site, Stereochemistry, Crystallography and Nuclear magnetic resonance. His Binding site study incorporates themes from Plasma protein binding and Nuclear magnetic resonance spectroscopy. His work focuses on many connections between Plasma protein binding and other disciplines, such as Proline, that overlap with his field of interest in Computational biology and PDZ domain.

His Stereochemistry study integrates concerns from other disciplines, such as Amino acid, Vancomycin, Antibiotics and Peptide. His Crystallography research includes elements of Dihedral angle, Hydrogen bond, Protein structure and Chemical shift. He combines subjects such as Chemical physics and Helix with his study of Chemical shift.

His most cited work include:

  • The Nuclear Overhauser Effect in Structural and Conformational Analysis (1102 citations)
  • The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains (1067 citations)
  • The structure and function of proline-rich regions in proteins. (789 citations)

What are the main themes of his work throughout his whole career to date?

Biochemistry, Crystallography, Stereochemistry, Chemical shift and Protein structure are his primary areas of study. His work carried out in the field of Crystallography brings together such families of science as Antiparallel, Molecule and Hydrogen bond. Michael P. Williamson works on Stereochemistry which deals in particular with Nuclear magnetic resonance spectroscopy.

His Nuclear magnetic resonance spectroscopy research incorporates elements of Dihedral angle and Two-dimensional nuclear magnetic resonance spectroscopy. His research investigates the connection between Chemical shift and topics such as Protein secondary structure that intersect with problems in Amide. His research ties Plasma protein binding and Binding site together.

He most often published in these fields:

  • Biochemistry (28.12%)
  • Crystallography (24.65%)
  • Stereochemistry (23.26%)

What were the highlights of his more recent work (between 2012-2021)?

  • Crystallography (24.65%)
  • Mutant (4.86%)
  • Chemical shift (15.28%)

In recent papers he was focusing on the following fields of study:

Michael P. Williamson mainly focuses on Crystallography, Mutant, Chemical shift, Microbiology and Biochemistry. His Crystallography research is multidisciplinary, relying on both Antiparallel, Bombyx mori, Ubiquitin and Ruthenium. His study in Antiparallel is interdisciplinary in nature, drawing from both Proton NMR, Stereochemistry and Intermolecular force.

His research integrates issues of Ramachandran plot, Protein structure, Hydrogen bond and Protein secondary structure in his study of Chemical shift. His research is interdisciplinary, bridging the disciplines of Nuclear magnetic resonance spectroscopy and Protein secondary structure. Michael P. Williamson combines Biochemistry and Cytochrome b6f complex in his studies.

Between 2012 and 2021, his most popular works were:

  • Using chemical shift perturbation to characterise ligand binding. (689 citations)
  • Molecular basis for bacterial peptidoglycan recognition by LysM domains. (103 citations)
  • Analysis of the Structure of Bombyx mori Silk Fibroin by NMR (75 citations)

In his most recent research, the most cited papers focused on:

  • Enzyme
  • Amino acid
  • Gene

The scientist’s investigation covers issues in Chemical shift, Crystallography, Biochemistry, Bombyx mori and Fibroin. His Chemical shift research is multidisciplinary, incorporating elements of Chemical physics, Barnase, Deuterium, Heteronuclear single quantum coherence spectroscopy and Amine gas treating. His studies examine the connections between Heteronuclear single quantum coherence spectroscopy and genetics, as well as such issues in Allosteric regulation, with regards to Binding site.

His Binding site study integrates concerns from other disciplines, such as Cell adhesion and Cell biology. The concepts of his Crystallography study are interwoven with issues in Antiparallel, Microsecond, Wild type, Excited state and Conformational isomerism. In the field of Biochemistry, his study on Protochlorophyllide and Synechocystis overlaps with subjects such as Cytochrome b6f complex, Photosystem I and Chlorophyll Binding Proteins.

Best Publications

  • The Nuclear Overhauser Effect in Structural and Conformational Analysis

    David Neuhaus;Michael P. Williamson

  • The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains

    Brian K. Kay;Michael P. Williamson;Marius Sudol

  • Using chemical shift perturbation to characterise ligand binding.

    Mike P. Williamson

  • The structure and function of proline-rich regions in proteins.

    M P Williamson

  • Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry.

    Michael P. Williamson;Timothy F. Havel;Kurt Wüthrich

  • Polyphenol/peptide binding and precipitation.

    Adrian J. Charlton;Nicola J. Baxter;M. Lokman Khan;Arthur J. G. Moir

  • MULTIPLE INTERACTIONS BETWEEN POLYPHENOLS AND A SALIVARY PROLINE-RICH PROTEIN REPEAT RESULT IN COMPLEXATION AND PRECIPITATION

    Nicola J. Baxter;Terence H. Lilley;Edwin Haslam;Michael P. Williamson

  • Temperature dependence of 1H chemical shifts in proteins

    Nicola J. Baxter;Michael P. Williamson

  • Refined crystal structure of Cd, Zn metallothionein at 2.0 A resolution.

    A H Robbins;D E McRee;M Williamson;S A Collett

  • POLYPHENOLS, ASTRINGENCY AND PROLINE-RICH PROTEINS

    Genevieve Luck;Hua Liao;Nicola J. Murray;Heidi R. Grimmer

  • Molecular model for astringency produced by polyphenol/protein interactions.

    Elisabeth Jöbstl;John O'Connell;J Patrick A Fairclough;Mike P Williamson

  • Rapid-pulsing artifacts in double-quantum-filtered COSY

    Andrew E Derome;Michael P Williamson

  • Pseudomonas cellulose-binding domains mediate their effects by increasing enzyme substrate proximity

    David N. Bolam;Antonio Ciruela;Simon McQUEEN-MASON;Peter Simpson

  • Study of the interaction between salivary proline-rich proteins and a polyphenol by 1H-NMR spectroscopy.

    Nicola J. Murray;Michael P. Williamson;Terence H. Lilley;Edwin Haslam

  • Analysis of Peptidoglycan Structure from Vegetative Cells of Bacillus subtilis 168 and Role of PBP 5 in Peptidoglycan Maturation

    Abdelmadjid Atrih;Gerold Bacher;Günter Allmaier;Michael P. Williamson

  • Epigallocatechin gallate, the main polyphenol in green tea, binds to the T-cell receptor, CD4: Potential for HIV-1 therapy.

    Mike P. Williamson;Theron G. McCormick;Christina L. Nance;William T. Shearer

  • Analysis of the Structure of Bombyx mori Silk Fibroin by NMR

    Tetsuo Asakura;Keiko Okushita;Mike P. Williamson

  • C alpha and C beta carbon-13 chemical shifts in proteins from an empirical database.

    Mitsuo Iwadate;Tetsuo Asakura;Michael P. Williamson

  • Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to β-cyclodextrin

    Kay Sorimachi;Marie Françoise Le Gal-Coëffet;Gary Williamson;David B. Archer

  • Molecular basis for bacterial peptidoglycan recognition by LysM domains.

    Stéphane Mesnage;Mariano Dellarole;Nicola J. Baxter;Jean Baptiste Rouget

  • Refined crystal structure of Cd, Zn metallothionein at 2.0Åresolution

    A.H. Robbins;D.E. McRee;M. Williamson;S.A. Collett

Frequent Co-Authors

Harry J. Gilbert
Harry J. Gilbert Newcastle University
Tetsuo Asakura
Tetsuo Asakura Tokyo University of Agriculture and Technology
Dudley H. Williams
Dudley H. Williams University of Cambridge
Gary Williamson
Gary Williamson Monash University
David N. Bolam
David N. Bolam Newcastle University
Edwin Haslam
Edwin Haslam University of Sheffield
Poul Erik Hansen
Poul Erik Hansen Roskilde University
Kazuyuki Akasaka
Kazuyuki Akasaka Kyoto Prefectural University of Medicine
Geoffrey P. Hazlewood
Geoffrey P. Hazlewood Babraham Institute
Jim A. Thomas
Jim A. Thomas University of Sheffield

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