Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Hydrogen bond stereochemistry in protein structure and function.

J A Ippolito¹, R S Alexander, D W Christianson

¹Department of Chemistry, University of Pennsylvania, Philadelphia 19104-6323.

Journal of Molecular Biology

|October 5, 1990

Summary

This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

A biochar selection method for remediating heavy metal contaminated mine tailings.

International journal of environmental science and technology : IJEST·2025

Same author

The Effects of Long-term Molybdenum Exposure in Drinking Water on Molybdenum Metabolism and Production Performance of Beef Cattle Consuming a High Forage Diet.

Biological trace element research·2023

Same author

Structural studies of geranylgeranylglyceryl phosphate synthase, a prenyltransferase found in thermophilic Euryarchaeota.

Acta crystallographica. Section D, Structural biology·2020

Same author

Biochar reduces the efficiency of nitrification inhibitor 3,4-dimethylpyrazole phosphate (DMPP) mitigating N<sub>2</sub>O emissions.

Scientific reports·2019

Same author

Analysis of pelvic fracture pattern and overall orthopaedic injury burden in children sustaining pelvic fractures based on skeletal maturity.

Journal of children's orthopaedics·2017

Same author

Biochars Reduce Mine Land Soil Bioavailable Metals.

Journal of environmental quality·2017

Same journal

DynaPIN: A tool for characterizing dynamic protein interfaces.

Journal of molecular biology·2026

Same journal

BindRNAgen: Protein-binding RNA sequence generation using latent diffusion models.

Journal of molecular biology·2026

Same journal

Structural basis of HSP90C, a highly active chloroplastic HSP90 chaperone from Arabidopsis thaliana.

Journal of molecular biology·2026

Same journal

Clinical inflammasome biomarkers: Progress and prospects.

Journal of molecular biology·2026

Same journal

Biologically Relevant, Cationic Residues in Human Rhinovirus Stabilize Capsid-Bound RNA Duplexes, and Restrict Capsid Flexibility.

Journal of molecular biology·2026

Same journal

Cryo-EM structures of phage T4 infection intermediate.

Journal of molecular biology·2026

See all related articles

This study analyzes recurring hydrogen bond stereochemistry in protein structures, revealing preferential bonding patterns for various amino acid side chains. Understanding these patterns is key to interpreting protein structure, function, and interactions.

Area of Science:

Biochemistry
Structural Biology
Protein Science

Background:

Previous studies have cataloged hydrogen bond statistics in proteins.
A detailed stereochemical analysis of hydrogen bond donors and acceptors within protein side chains is lacking.

Purpose of the Study:

To analyze recurring motifs in hydrogen bond stereochemistry for amino acid side chains in proteins.
To provide a detailed stereochemical analysis of hydrogen bond donors and acceptors.

Main Methods:

Analysis of 50 high-resolution protein structures from the Brookhaven Protein Data Bank.
Identification and characterization of hydrogen bond stereochemistry for specific amino acid side chains.

Main Results:

Related Experiment Videos

Identified preferential hydrogen bond stereochemistry for side chains including glutamate, aspartate, glutamine, asparagine, arginine, histidine, tryptophan, tyrosine, lysine, serine, threonine, cysteine, methionine, and cystine.

Demonstrated that hydrogen bond stereochemistry is governed by acceptor atom electronics, donor atom steric accessibility, and side chain conformation.

Conclusions:

Preferential hydrogen bond stereochemistry in proteins is predictable and influenced by electronic and steric factors.
Understanding protein hydrogen bond stereochemistry is crucial for interpreting protein structure, function, stability, molecular recognition, and biological catalysis.