Computational analysis of N-H鈰€ interactions and its impact on the structural stability of 尾-lactamases
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- 作者：P. Lavanya ; Sudha Ramaiah ; An ; Anbarasu
- 关键词：Ala (A) ; Alanine ; Arg (R) ; Arginine ; Asn (N) ; Asparagine ; Asp (D) ; Aspartic acid ; Cys (C) ; Cysteine ; Gln (Q) ; Glutamine ; Glu (E) ; Glutamic acid ; Gly (G) ; Glycine ; HBAT ; Hydrogen Bond Analysis Tool ; His (H) ; Histidine ; Ile (I) ; Isoleucine ; Leu (L) ; Leucine ; Lys (K) ; Lysine ; Met (M) ; Methionine ; Phe (F) ; Phenylalanine ; Pro (P) ; Proline ; PDB ; Protein data bank ; SASA ; Solvent accessible surface area ; SC ; Stabilization center ; Ser (S) ; Serine ; Thr (T) ; Threonine ; Trp (W) ; Tryptophan ; Tyr (Y) ; Tyrosin
- 刊名：Computers in Biology and Medicine
- 出版年：1 March, 2014
- 年：2014
- 卷：46
- 期：Complete
- 页码：22-28
- 全文大小：1531 K
文摘
Studies on intra-protein interactions provide valuable information on protein conformation. The aim of our study is to explore the functional importance of residues participating in N-H鈰€ hydrogen bonds in maintaining the conformational stability of 尾-lactamases. Our results show that most of the residues participating in N-H鈰€ hydrogen bond formation are functionally important and play a significant role in stabilizing the structure with more than one stabilizing region. Our findings reveal the importance of N-H鈰€ hydrogen bonds in the stability of 尾-lactamases. These findings may be helpful for medicinal and computational protein chemists working in the area of enzyme mediated antibiotic resistance.