Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Small x Assumption02:20

The Small x Assumption

If a reaction has a small equilibrium constant, the equilibrium position favors the reactants. In such reactions, a negligible change in concentration may occur if the initial concentrations of reactants are high and the Kc value is small. In such circumstances, the equilibrium concentration is approximately equal to its initial concentration. This estimation can be used to simplify the equilibrium calculations by assuming that some equilibrium concentrations are equal to the initial...
Radical Chain-Growth Polymerization: Chain Branching01:17

Radical Chain-Growth Polymerization: Chain Branching

The skeletal structure of polymers synthesized via radical polymerization is always branched. For example, the polymerization of ethylene by radical polymerization results in a low-density grade of polyethylene with a heavily branched skeletal structure. Here, the radical site abstracts hydrogen from the growing chain, and the radical site shifts from the end (a primary carbon center) to anywhere within the growing chain (a secondary carbon center). Consequently, the part of the chain from the...
Consecutive Reactions01:22

Consecutive Reactions

Consecutive reactions involve a sequence where the product of a preceding reaction becomes the reactant for the subsequent one. In a simple scheme, A transforms into B, which further reacts to form C, with rate constants k1 and k2, respectively. This concept is evident in the radioactive decay series. Assuming an initial state with only A present, the conservation of matter leads to three coupled differential equations, determining the concentrations of A, B, and C over time.The rate of change...
Continuity of a Function01:23

Continuity of a Function

A function is continuous at a point a if three conditions are met: the function is defined at a, the limit of the function as x approaches a exists, and this limit equals the function’s value. Mathematically, this is written asThis definition ensures the graph of the function does not exhibit any breaks, holes, or jumps at that point. Discontinuities occur when any of these conditions fail. A removable discontinuity exists when the two-sided limit exists but the function is either undefined or...
Convergence of Sequences01:26

Convergence of Sequences

A sequence is a function defined on the natural numbers that assigns a value to each index. It can be understood as an ordered list of terms generated one after another. In mathematical analysis, an important question is whether the terms of a sequence approach a single real number as the index becomes very large. When this happens, the sequence is said to converge, and the value approached is called the limit. From a graphical perspective, convergence means that the plotted terms approach a...
Continuity for Functions of Multiple Variables01:27

Continuity for Functions of Multiple Variables

Continuity in multivariable functions extends the concept familiar from single-variable calculus into higher dimensions, where a function's output depends on two or more input variables. This generalization is crucial in modeling real-world phenomena across spatial domains. A multivariable function is considered continuous at a point if three conditions are simultaneously satisfied: the function is defined at that point, the limit of the function exists as the input approaches the point from...

You might also read

Related Articles

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

Sort by
Same author

Increased activity of DRD1-MSNs in dorsolateral striatum underlies Cry1Δ11 mutation-induced repetitive behaviors.

Translational psychiatry·2026
Same author

Topology Switching in Polymetallic Fragments Governed by Metal Encapsulation.

Journal of the American Chemical Society·2026
Same author

Mechanism of Aggregation of the NACore of α-Synuclein: Stable Oligomer Formation Competes with Fibril Formation with Implications for the Etiology of Parkinson's Disease.

Journal of the American Chemical Society·2026
Same author

Mechanism of Photoinduced Conformational Changes in the Photoenzyme Fatty Acid Photodecarboxylase Revealed by Light- Footprinting Ion Mobility Mass Spectrometry.

Journal of the American Chemical Society·2026
Same author

Root Cause Determination for Customer Complaint Biopharmaceutical Drug Product Samples with Abnormal Appearance.

PDA journal of pharmaceutical science and technology·2026
Same author

A Novel Heterometallic Ring {Cr<sub>5</sub>Ni<sub>3</sub>} and New {Cr<sub>6</sub>Co<sub>2</sub>} and {Cr<sub>6</sub>Zn<sub>2</sub>} Rings.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Related Experiment Video

Updated: Jul 9, 2026

Subcloning Plus Insertion (SPI) - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors
09:02

Subcloning Plus Insertion (SPI) - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors

Published on: January 8, 2015

Sequential hydration of small protonated peptides.

Dengfeng Liu1, Thomas Wyttenbach, Perdita E Barran

  • 1Department of Chemistry and Biochemistry, University of California at Santa Barbara, Santa Barbara, California 93106, USA.

Journal of the American Chemical Society
|July 10, 2003
PubMed
Summary

Water molecules bind more strongly to the first site of protonation on small peptides and at higher charge states. Binding strength decreases with subsequent water molecules and is weaker for arginine-containing peptides.

More Related Videos

Operation of the Collaborative Composite Manufacturing (CCM) System
10:09

Operation of the Collaborative Composite Manufacturing (CCM) System

Published on: October 1, 2019

Precision Induction and Distinction of Coughing and Sneezing Reflexes in Mice
09:30

Precision Induction and Distinction of Coughing and Sneezing Reflexes in Mice

Published on: October 3, 2025

Related Experiment Videos

Last Updated: Jul 9, 2026

Subcloning Plus Insertion (SPI) - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors
09:02

Subcloning Plus Insertion (SPI) - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors

Published on: January 8, 2015

Operation of the Collaborative Composite Manufacturing (CCM) System
10:09

Operation of the Collaborative Composite Manufacturing (CCM) System

Published on: October 1, 2019

Precision Induction and Distinction of Coughing and Sneezing Reflexes in Mice
09:30

Precision Induction and Distinction of Coughing and Sneezing Reflexes in Mice

Published on: October 3, 2025

Area of Science:

  • Physical Chemistry
  • Computational Chemistry
  • Biophysics

Background:

  • Understanding peptide hydration is crucial for fields like drug design and protein folding.
  • Protonated peptides in solution interact with water molecules, influencing their structure and behavior.

Purpose of the Study:

  • To investigate the sequential binding of water molecules to protonated peptides.
  • To quantify water binding energies and identify trends in peptide hydration.

Main Methods:

  • Equilibrium experiments using electrospray ionization and drift cell techniques.
  • Comparison of experimental data with molecular mechanics simulations of hydrated peptide structures.

Main Results:

  • Water binding energies range from 7-15 kcal/mol, with the first water molecule binding strongest.
  • Smaller peptides and higher charge states exhibit stronger initial water binding.
  • Water binds less strongly to protonated guanidino groups (arginine) than amino groups.
  • Water addition is highly dependent on peptide charge state and weakly on peptide sequence.

Conclusions:

  • The initial hydration of peptides is dominated by strong interactions at the protonation site.
  • As solvation shells form, subsequent water molecules bind less strongly and can interact with remote sites.
  • Peptide charge state and size significantly dictate hydration patterns and binding affinities.