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Study of lamprin structure by Circular dichroism (CD) (CAT#: STEM-MB-0620-WXH)

Introduction

In molecular biology, the lamprin family of proteins consists of several lamprin proteins from the Sea lamprey Petromyzon marinus. Lamprin, an insoluble non-collagen, non-elastin protein, is the major connective tissue component of the fibrillar extracellular matrix of lamprey annular cartilage. Although not generally homologous to any other protein, soluble lamprins contain a tandemly repeated peptide sequence (GGLGY), which is present in both silk moth chorion proteins and spider dragline silk. Strong homologies to this repeat sequence are also present in several mammalian and avian elastins. It is thought that these proteins share a structural motif which promotes self-aggregation and fibril formation in proteins through interdigitation of hydrophobic side chains in beta-sheet/beta-turn structures.




Principle

Circular dichroism (CD) is a spectroscopy technique that measures the absorption difference between left and right circularly polarized light. By symmetry, this asymmetric absorption can only occur for asymmetric molecules, meaning chiral molecules.

Applications

Circular dichroism (CD) spectroscopy is a powerful technique that is sensitive to the chirality (handedness) of molecules. It can be used to study absolute stereochemistry, enantiomeric composition, racemization, enantiomeric differentiation, and molecular interactions and conformation.

Procedure

1. Sample preparation
2. Measurement by CD instrument
3. Data analysis

Materials

Circular dichroism (CD) spectrophotometer
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