NDLI: Assisted Peptide Folding by Surface Pattern Recognition

Content Provider	PubMed Central
Author	Zhuang, Zhuoyun Jewett, Andrew I. Silvan, Kuttimalai Giovanni, Bellesia Gnanakaran, S. Shea, Joan-emma
Copyright Year	2011
Abstract	Natively disordered proteins belong to a unique class of biomolecules whose function is related to their flexibility and their ability to adopt desired conformations upon binding to substrates. In some cases these proteins can bind multiple partners, which can lead to distinct structures and promiscuity in functions. In other words, the capacity to recognize molecular patterns on the substrate is often essential for the folding and function of intrinsically disordered proteins. Biomolecular pattern recognition is extremely relevant both in vivo (e.g., for oligomerization, immune response, induced folding, substrate binding, and molecular switches) and in vitro (e.g., for biosensing, catalysis, chromatography, and implantation). Here, we use a minimalist computational model system to investigate how polar/nonpolar patterns on a surface can induce the folding of an otherwise unstructured peptide. We show that a model peptide that exists in the bulk as a molten globular state consisting of many interconverting structures can fold into either a helix-coil-helix or an extended helix structure in the presence of a complementary designed patterned surface at low hydrophobicity (3.7%) or a uniform surface at high hydrophobicity (50%). However, we find that a carefully chosen surface pattern can bind to and catalyze the folding of a natively unfolded protein much more readily or effectively than a surface with a noncomplementary or uniform distribution of hydrophobic residues.
Related Links	http://dx.doi.org/10.1016/j.bpj.2010.12.3735
Ending Page	1315
Page Count	10
Starting Page	1306
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	5
Volume Number	100
Language	English
Publisher	The Biophysical Society
Publisher Date	2011-03-01
Access Restriction	Open
Rights Holder	The Biophysical Society
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Thermodynamic Characterization of the Folding Coupled DNA Binding by the Monomeric Transcription Activator GCN4 Peptide

A Directed Essential Dynamics Simulation of Peptide Folding

Insight into the Folding Inhibition of the HIV-1 Protease by a Small Peptide

Studies on protein folding by ribosome

Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide.

Secondary Structure Propensities in Peptide Folding Simulations: A Systematic Comparison of Molecular Mechanics Interaction Schemes

Kinetics of Peptide Folding in Lipid Membranes

Generalized Pattern Search Algorithm for Peptide Structure Prediction

Substrate recognition by gelatinase A: the C-terminal domain facilitates surface diffusion.

Assisted Peptide Folding by Surface Pattern Recognition

Similar Documents

Thermodynamic Characterization of the Folding Coupled DNA Binding by the Monomeric Transcription Activator GCN4 Peptide

A Directed Essential Dynamics Simulation of Peptide Folding

Insight into the Folding Inhibition of the HIV-1 Protease by a Small Peptide

Studies on protein folding by ribosome

Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide.

Secondary Structure Propensities in Peptide Folding Simulations: A Systematic Comparison of Molecular Mechanics Interaction Schemes

Kinetics of Peptide Folding in Lipid Membranes

Generalized Pattern Search Algorithm for Peptide Structure Prediction

Substrate recognition by gelatinase A: the C-terminal domain facilitates surface diffusion.

Assisted Peptide Folding by Surface Pattern Recognition