The Ac-RGD-NH2 peptide as a probe of slow conformational exchange of short linear peptides in DMSO-Reference-Cited by-同舟云学术

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The Ac-RGD-NH2 peptide as a probe of slow conformational exchange of short linear peptides in DMSO

Published:2003-04-21 Issue:1 Volume:69 Page:72-86
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Biris Nikolaos,Stavrakoudis Athanassios,Politou Anastasia S.,Mikros Emmanuel,Sakarellos-Daitsiotis Maria,Sakarellos Constantinos,Tsikaris Vassilios

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference36 articles.

1. Structure of the fibrinogen binding sequence: arginylglycylaspartic acid (RGD)

2. Preferred conformations of a linear RGD tripeptide

3. The effect of conformation on the solution stability of linear vs. cyclic RGD peptides

4. A crystal molecular conformation of leucine-enkephalin related to the morphine molecule

5. Relationship of the crystal and molecular structure of leucine-enkephalin trihydrate to that of morphine

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2. A highly constrained cyclic (S,S)-CDC- peptide is a potent inhibitor of carotid artery thrombosis in rabbits;Platelets;2010-12-15

3. Terminal-specific PEGylation of polypeptides in a dilute solution;Journal of Applied Polymer Science;2010-07-13

4. Conformational Studies of the 313-320 and 313-332 Peptide Fragments Derived from the αIIb Subunit of Integrin Receptor with Molecular Dynamics Simulations;International Journal of Peptide Research and Therapeutics;2009-07-24

5. Insights into the structure of the PmrD protein with molecular dynamics simulations;International Journal of Biological Macromolecules;2009-06

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