Forces behind N- and C-capping of peptidic helices

Helical peptides are primarily stabilized by intramolecular hydrogen bonds. Particular conformational arrangements, capping motifs, help precisely terminate helices by compensating for disruption of helical H-bonding patterns. This contribution explores if: (i) N-and C-caps are essentially the same; and, (ii) how differences impact their thermodynamic helix stabilities and folding kinetics.

Institutions

Publication Details

Journal
Chemical Communications
Published
2025-12-08
DOI
https://doi.org/10.1039/d5cc04856g
Primary Topic
Chemical Synthesis and Analysis
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Forces behind N- and C-capping of peptidic helices

Chemical Communications
Chemical Synthesis and Analysis
article

Forces behind N- and C-capping of peptidic helices

article en

Abstract

Helical peptides are primarily stabilized by intramolecular hydrogen bonds. Particular conformational arrangements, capping motifs, help precisely terminate helices by compensating for disruption of helical H-bonding patterns. This contribution explores if: (i) N-and C-caps are essentially the same; and, (ii) how differences impact their thermodynamic helix stabilities and folding kinetics.

Chemical CommunicationsVol. 62(9)
University of Konstanz (DE), Texas A&M University (US)
Openalex Percentile: Top 41%
Chemical Synthesis and Analysis
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

Forces behind N- and C-capping of peptidic helices · Chemical Communications (2025) | TGRS Research Map | TGRS