A precise and accurate method of measuring Kendrew model coordinates | Zendy

Frentrup M. A. | Zendy; Tulinsky A. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

A precise and accurate method of measuring Kendrew model coordinates

Author(s) -

Frentrup M. A.,

Tulinsky A.

Publication year - 1981

Publication title -

journal of applied crystallography

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.429

H-Index - 162

ISSN - 1600-5767

DOI - 10.1107/s0021889881009722

Subject(s) - standard deviation , polar coordinate system , dimer , chemistry , absolute deviation , dihedral angle , polar , bipolar coordinates , log polar coordinates , orthogonal coordinates , molecule , mathematical analysis , physics , hydrogen bond , mathematics , geometry , nuclear magnetic resonance , statistics , organic chemistry , astronomy

Polar coordinates of a Kendrew model of α‐chymotrypsin (α‐CHT) have been measured with a surveyor's transit and a cathetometer to a high degree of accuracy and precision. Bond distances calculated independently for more than 200 independent amino‐acid residues have standard deviations of 0.10 Å or less, the torsion angle ω has a standard error of 7°, and the τ angle is precise to 3°. The measured coordinates of about 1800 non‐hydrogen atoms of one molecule of the α‐CHT dimer fit a set of idealized polypeptide coordinates with a r.m.s. deviation of 0.17 Å, while the average deviation is 0.15 Å.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research