𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Geometrical and Sequence Characteristics of α-Helices in Globular Proteins

✍ Scribed by Kumar, Sandeep; Bansal, Manju

Book ID
119411491
Publisher
Biophysical Society
Year
1998
Tongue
English
Weight
170 KB
Volume
75
Category
Article
ISSN
0006-3495

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Dissecting α-helices: Position-specific
Dissecting α-helices: Position-specific analysis of α-helices in globular proteins
✍ Sandeep Kumar; Manju Bansal 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 258 KB 👁 1 views

An analysis of the amino acid distributions at 15 positions, viz., NЉ, NЈ, Ncap, N1, N2, N3, N4, Mid, C4, C3, C2, C1, Ccap, CЈ, and CЉ in 1,131 ␣-helices reveals that each position has its own unique characteristics. In general, natural helix sequences optimize by identifying the residues to be avoi

Correlation of sequence and tertiary str
Correlation of sequence and tertiary structure in globular proteins
✍ Gordon M. Crippen 📂 Article 📅 1977 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 711 KB

## Abstract The x‐ray crystal structures of 19 selected proteins are examined empirically for correlations between the amino acid sequence and long‐range, __tertiary__ conformation. There is clear evidence for preferential associations of certain types of amino acids, particularly among the hydroph

The structure of the ends of α-helices i
The structure of the ends of α-helices in globular proteins: Effect of additional hydrogen bonds and implications for helix formation
✍ David P. Leader; E. James Milner-White 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 451 KB

## Abstract We prepared a set of about 2000 α‐helices from a relational database of high‐resolution three‐dimensional structures of globular proteins, and identified additional main chain __i__ ← __i__+3 hydrogen bonds at the ends of the helices (i.e., where the hydrogen bonding potential is not fu